Lorenzo Napolitano - Academia.edu (original) (raw)

Papers by Lorenzo Napolitano

Research paper thumbnail of Purification, biochemical characterization and cloning of a new cationic peroxidase isoenzyme from artichoke

Plant Physiology and Biochemistry, Apr 1, 2011

A cationic soluble peroxidase isoenzyme (CysPrx) has been purified and characterized from articho... more A cationic soluble peroxidase isoenzyme (CysPrx) has been purified and characterized from artichoke (Cynara cardunculus subsp. scolymus (L.) Hegi) leaves by combination of aqueous two phase extraction, ion exchange chromatography, and gel filtration. The purification fold was 149 and the activity recovery 5.5%. CysPrx was stable from 5 to 45 °C with a pH optimum around 5.5; the pI was 8.3

Research paper thumbnail of Preliminary characterization of a bacteriolysin-like protein produced by a cheese-isolated L. lactis strain

Research paper thumbnail of Evidence for a common epitope between bovine alpha-lactalbumin and beta-lactoglobulin

Biological chemistry, 1998

The aim of this work was to check and quantify any cross-reactivities among the main bovine whey ... more The aim of this work was to check and quantify any cross-reactivities among the main bovine whey proteins, utilizing purified polyclonal antibodies against bovine beta-lactoglobulin, alpha-lactalbumin and serum albumin, and to identify possible common epitope(s). Purified polyclonal anti-bovine beta-lactoglobulin antibodies show 10% cross-reactivity with bovine alpha-lactalbumin, both in its native and its denatured form. A continuous stretch of four amino acids common to alpha-lactalbumin and beta-lactoglobulin that might be responsible for this cross-reactivity has been identified. Cross-reactivity between this antibody and bovine serum albumin is, on the contrary, negligible. Purified polyclonal anti-bovine alpha-lactalbumin and anti-serum albumin antibodies do not cross-react.

Research paper thumbnail of The Amino-Acid Sequence of Two Isoforms of α-Lactalbumin from Donkey(Equus asinus)Milk is Identical

Biological Chemistry Hoppe-Seyler, 1992

The complete primary structure of donkey α-lactalbumin A and B has been determined by sequencing ... more The complete primary structure of donkey α-lactalbumin A and B has been determined by sequencing of the peptides obtained after tryptic, Glu-C proteinase or cyanogen bromide cleavage. Although preparative purification of α-lactalbumin by flat-bed isoelectric focusing gave two protein fractions A and B, their amino-acid sequence revealed no differences. Donkey α-lactalbumin shows two, four and five differences in comparison to the horse a-lactalbumin A, B and C.Thus donkey α-lactalbumin is homogeneous and belongs to the horse Α-type variant. Die Aminos uresequenz zweier Isoformen des a-Lactalbumins aus Eselsmilch ist identisch Zusammenfassung: Die vollst ndige Prim rstruktur von α-Lactalbumin Aund B des Esels wurde durch Sequenzierung der Peptide nach tryptischer, Glu-C-Proteinase-oder Cyanogenbromid-Spaltung erhalten. Obwohl die pr parative Reinigung von a-Lactalbumin durch Flachbett-Isoelektrofokussierung zwei Proteinfraktionen (A und B) ergab, zeigte ihre Key terms: α-Lactalbumin, primary structure, Ca 2 ® binding.

Research paper thumbnail of Human milk components cross‐reacting with antibodies against bovine β‐lactoglobulin

Acta Paediatrica, 1992

The human whey components cross‐reacting with antibodies raised against bovine and/or equine β‐la... more The human whey components cross‐reacting with antibodies raised against bovine and/or equine β‐lactoglobulin were screened systematically. The milk of six women on a normal diet was collected within 72 h of confinement and whey components were fractionated by high‐speed size exclusion chromatography and reversed‐phase techniques. The fractions which were immunoreactive in double diffusion experiments with antisera anti‐bovine and/or equine β‐lactoglobulin were subsequently purified by native PAGE and then electroblotted on Pro‐blott membrane (Western blotting). Pro‐blot membranes were stained in parallel with Coomassie and by immunostaining using antibodies against bovine and/or equine β‐lactoglobulin as first antibody solution. The immunoreactive bands were cut out from the membrane and N‐terminally sequenced; all the immunoreactive components were clearly identified as human β‐casein or its (mainly tryptic) fragments. The strong antigenic similarity between human β‐casein and β‐la...

Research paper thumbnail of Isolation of Donkey Whey Proteins and N-Terminal Amino-Acid Sequence of Alpha-Lactalbumin-A and Alpha-Lactalbumin-B, Beta-Lactoglobulin-I and Beta-Lactoglobulin-II and Lysozyme

Milchwissenschaft-milk Science International, 1989

Structures, fonctions et evolution des proteines du lactoserum de lait d'ânesse en relation a... more Structures, fonctions et evolution des proteines du lactoserum de lait d'ânesse en relation avec la genetique

Research paper thumbnail of Comparative study of casein content in human colostrum and milk

Milchwissenschaft-milk Science International, 1994

Research paper thumbnail of A pr 2 01 8 Technology networks : the autocatalytic origins of innovation

We analyse the autocatalytic structure of technological networks and evaluate its significance fo... more We analyse the autocatalytic structure of technological networks and evaluate its significance for the dynamics of innovation patenting. To this aim, we define a directed network of technological fields based on the International Patents Classification, in which a source node is connected to a receiver node via a link if patenting activity in the source field anticipates patents in the receiver field in the same region more frequently than we would expect at random. We show that the evolution of the technology network is compatible with the presence of a growing autocatalytic structure, i.e. a portion of the network in which technological fields mutually benefit from being connected to one another. We further show that technological fields in the core of the autocatalytic set display greater fitness, i.e. they tend to appear in a greater number of patents, thus suggesting the presence of positive spillovers as well as positive reinforcement. Finally, we observe that core shifts take...

Research paper thumbnail of Separation of Whey Proteins from Llama (Lama-Glama L) Milk - Identification of a Protein Immunologically Related to Beta-Lactoglobulins

Separation of llama whey proteins by size exclusion HPLC followed by purification through prepara... more Separation of llama whey proteins by size exclusion HPLC followed by purification through preparative IEF and reversed phase HPLC led to the isolation of a protein reacting with polyclonal antibody anti-bovine beta-lactoglobulin in an immuno double diffusion experiment.The N-terminal amino acid sequence of this llama whey protein showed some homology with internal parts of human k-casein and human lactotransferrin as well as an interesting identity with recognized beta-lactoglobulins in positions Pro 4 and Leu 10.

Research paper thumbnail of Isolation of donkey whey proteins and N-terminal amino acid sequence of α-lactalbumins A and B, β-lactoglobulins I and II and lyzozyme

Structures, fonctions et evolution des proteines du lactoserum de lait d'ânesse en relation a... more Structures, fonctions et evolution des proteines du lactoserum de lait d'ânesse en relation avec la genetique

Research paper thumbnail of Identification and Characterization of 2 Alpha-Lactalbumins from Somali Camel Milk (Camelus-Dromedarius)

Milchwissenschaft-milk Science International, 1985

Composition en acides amines et identification de la sequence N-terminale de deux formes d'α-... more Composition en acides amines et identification de la sequence N-terminale de deux formes d'α-lactalbumine isolees de lait de chamelle par chromatographie sur gel

Research paper thumbnail of Amino acid sequence and crystal structure of buffalo α-lactalbumin

FEBS Letters, 1996

Isolation, purification, amino acid sequence determination and X-ray crystal structure of buffalo... more Isolation, purification, amino acid sequence determination and X-ray crystal structure of buffalo alpha-lactalbumin were performed in order to gain further knowledge of the molecular basis of alpha-lactalbumin in the lactose synthase complex. The deduced amino acid sequence differs at one position from the bovine alpha-lactalbumin sequence (at position 17). The refined crystal structure at 2.3 A is very similar to those previously reported for human and baboon alpha-lactalbumins. However, a portion of the molecule (residues 105-109) exhibits different conformation. It forms a 'flexible loop', and appears to be a functionally important region in forming the lactose synthase complex.

Research paper thumbnail of Effects of two different domestic boiling practices on the allergenicity of cow's milk proteins

Journal of the Science of Food and Agriculture

Research paper thumbnail of Identification of Equine Lactadherin-Derived Peptides that Inhibit Rotavirus Infection via Integrin Receptor Competition

The Journal of biological chemistry, Jan 26, 2015

Human rotavirus is the leading cause of severe gastroenteritis in infants and children under the ... more Human rotavirus is the leading cause of severe gastroenteritis in infants and children under the age of five years in both developed and developing countries. Human lactadherin, a milk-fat globule membrane (MFGM) glycoprotein, inhibits human rotavirus infection in vitro, whereas bovine lactadherin is not active. Moreover, it protects breastfed infants against symptomatic rotavirus infections. To explore the potential antiviral activity of lactadherin sourced by equines we undertook a proteomic analysis of MFGM proteins from donkey milk and elucidated its amino acid sequence. Alignment of the human, bovine and donkey lactadherin sequences revealed the presence of an Asp-Gly-Glu (DGE) α2β1 integrin-binding motif in the N-terminal domain of donkey sequence only. Since integrin α2β1 plays a critical role during early steps of rotavirus host cell adhesion, we tested a mini-library of donkey lactadherin-derived peptides containing DGE sequence for anti-rotavirus activity. A 20 amino acid ...

Research paper thumbnail of The unusual amino acid triplet Asn-Ile-Cys is a glycosylation consensus site in human alpha-lactalbumin

Journal of protein chemistry, 1997

Human alpha-lactalbumin has not been described as a glycoprotein, despite the fact that several a... more Human alpha-lactalbumin has not been described as a glycoprotein, despite the fact that several alpha-lactalbumins of both ruminant and nonruminant species are known to be glycosylated. In all these species the glycosylation site is the 45Asn in the usual triplet 45Asn-Gly/Gln-47Ser. We have found that human alpha-lactalbumin is glycosylated and the glycosylation site has been determined by protein sequencing and mass spectrometry. We report an unusual glycosylation site at 71Asn in the triplet 71Asn-Ile-73Cys, which is conserved in all known alpha-lactalbumins except red-necked wallaby. That a relatively small proportion of the protein is glycosylated (about 1%) may reflect the importance of this region of the protein sequence to the molten globule state of alpha-lactalbumin.

Research paper thumbnail of Microanalysis of the Amino-Acid Sequence of Monomeric β-Lactoglobulin I from Donkey ( Equus asinus ) milk. The Primary Structure and its Homology with a Superfamily of Hydrophobic Molecule Transporters

Biological Chemistry Hoppe-Seyler, 1988

The complete primary structure of donkey beta-lactoglobulin I was determined by pulsed-liquid pha... more The complete primary structure of donkey beta-lactoglobulin I was determined by pulsed-liquid phase microsequencing of tryptic peptides. The protein has been isolated in monomeric form and it corresponds to monomeric beta-lactoglobulin of type I. With the inclusion of donkey beta-lactoglobulin I there are 13% common residues amongst the members of the beta-lactoglobulin family. Donkey beta-lactoglobulin I is homologous to the retinol-binding protein, bilin-binding protein and five other proteins belonging to the new superfamily of hydrophobic molecule transporters. A rapid method for peptide isolation and the strategy for microsequencing of this protein have been described.

Research paper thumbnail of The Primary Structure of Donkey (Equus asinus) Lysozyme contains the Ca(II) Binding Site of α-Lactalbumin

Biological Chemistry Hoppe-Seyler, 1988

The complete primary structure of donkey lysozyme has been established by pulsed liquid-phase seq... more The complete primary structure of donkey lysozyme has been established by pulsed liquid-phase sequencing of tryptic and chymotryptic peptides isolated by RP-HPLC. The positions of the Cys residues were identified by labeling the Cys residues with DABIA-reagent. Donkey lysozyme is a c-type lysozyme which is 129 amino acids long. It exhibits 50% homology to the human protein. We observe the full Ca(II) binding site suggested for the homologous alpha-lactalbumines. Although horse lysozyme has been reported to contain asparagine in position 61, which was in conflict with the three-dimensional structure of lysozyme, all other known c-type lysozymes, including donkey, contain Ser 61.

Research paper thumbnail of The Complete Primary Structure of α-Lactalbumin Isolated from Pig (Sus scrofa) Milk

Biological Chemistry Hoppe-Seyler, 1990

... USA 59, 491-497. Teahan, CG, McKenzie, HA & Shaw, DC (1986) llth Annual Conference on... more ... USA 59, 491-497. Teahan, CG, McKenzie, HA & Shaw, DC (1986) llth Annual Conference on Protein Structure and Function, Lome, Australia, Abstract. ... Dr. Amedeo Conti and Lorenzo Napolitano, Centro Studi Alimentazione Animali, CNR, Via P. Giuria 6.1-10125Torino, Italy. ...

Research paper thumbnail of The Complete Amino-Acid Sequence of Dimeric β-Lactoglobulin from Mouflon (Ovis ammon musimon) Milk

Biological Chemistry Hoppe-Seyler, 1987

... The Complete Amino-Acid Sequence of Dimeric /3-Lactoglobulin from Mouflon (Ovis ammon musimon... more ... The Complete Amino-Acid Sequence of Dimeric /3-Lactoglobulin from Mouflon (Ovis ammon musimon) Milk Jasminka GODOVAC-ZIMMERMANN*, Amedeo CoNTib and Lorenzo NAPOLITANO5 ... 9 Bell, K. & McKenzie, HA (1964) Nature (London) 204, 1275-1279. ...

Research paper thumbnail of Covalent Structure of the Minor Monomeric β-Lactoglobulin II Component from Donkey Milk

Biological Chemistry Hoppe-Seyler, 1990

Summary: The complete primary structure of the minor /3-lactoglobulin II component from donkey mi... more Summary: The complete primary structure of the minor /3-lactoglobulin II component from donkey milk is presented. It has been established by amino-acid sequencing and mass-spectrometry analysis of in-tact protein and peptides obtained after enzymatic and chemical ...

Research paper thumbnail of Purification, biochemical characterization and cloning of a new cationic peroxidase isoenzyme from artichoke

Plant Physiology and Biochemistry, Apr 1, 2011

A cationic soluble peroxidase isoenzyme (CysPrx) has been purified and characterized from articho... more A cationic soluble peroxidase isoenzyme (CysPrx) has been purified and characterized from artichoke (Cynara cardunculus subsp. scolymus (L.) Hegi) leaves by combination of aqueous two phase extraction, ion exchange chromatography, and gel filtration. The purification fold was 149 and the activity recovery 5.5%. CysPrx was stable from 5 to 45 °C with a pH optimum around 5.5; the pI was 8.3

Research paper thumbnail of Preliminary characterization of a bacteriolysin-like protein produced by a cheese-isolated L. lactis strain

Research paper thumbnail of Evidence for a common epitope between bovine alpha-lactalbumin and beta-lactoglobulin

Biological chemistry, 1998

The aim of this work was to check and quantify any cross-reactivities among the main bovine whey ... more The aim of this work was to check and quantify any cross-reactivities among the main bovine whey proteins, utilizing purified polyclonal antibodies against bovine beta-lactoglobulin, alpha-lactalbumin and serum albumin, and to identify possible common epitope(s). Purified polyclonal anti-bovine beta-lactoglobulin antibodies show 10% cross-reactivity with bovine alpha-lactalbumin, both in its native and its denatured form. A continuous stretch of four amino acids common to alpha-lactalbumin and beta-lactoglobulin that might be responsible for this cross-reactivity has been identified. Cross-reactivity between this antibody and bovine serum albumin is, on the contrary, negligible. Purified polyclonal anti-bovine alpha-lactalbumin and anti-serum albumin antibodies do not cross-react.

Research paper thumbnail of The Amino-Acid Sequence of Two Isoforms of α-Lactalbumin from Donkey(Equus asinus)Milk is Identical

Biological Chemistry Hoppe-Seyler, 1992

The complete primary structure of donkey α-lactalbumin A and B has been determined by sequencing ... more The complete primary structure of donkey α-lactalbumin A and B has been determined by sequencing of the peptides obtained after tryptic, Glu-C proteinase or cyanogen bromide cleavage. Although preparative purification of α-lactalbumin by flat-bed isoelectric focusing gave two protein fractions A and B, their amino-acid sequence revealed no differences. Donkey α-lactalbumin shows two, four and five differences in comparison to the horse a-lactalbumin A, B and C.Thus donkey α-lactalbumin is homogeneous and belongs to the horse Α-type variant. Die Aminos uresequenz zweier Isoformen des a-Lactalbumins aus Eselsmilch ist identisch Zusammenfassung: Die vollst ndige Prim rstruktur von α-Lactalbumin Aund B des Esels wurde durch Sequenzierung der Peptide nach tryptischer, Glu-C-Proteinase-oder Cyanogenbromid-Spaltung erhalten. Obwohl die pr parative Reinigung von a-Lactalbumin durch Flachbett-Isoelektrofokussierung zwei Proteinfraktionen (A und B) ergab, zeigte ihre Key terms: α-Lactalbumin, primary structure, Ca 2 ® binding.

Research paper thumbnail of Human milk components cross‐reacting with antibodies against bovine β‐lactoglobulin

Acta Paediatrica, 1992

The human whey components cross‐reacting with antibodies raised against bovine and/or equine β‐la... more The human whey components cross‐reacting with antibodies raised against bovine and/or equine β‐lactoglobulin were screened systematically. The milk of six women on a normal diet was collected within 72 h of confinement and whey components were fractionated by high‐speed size exclusion chromatography and reversed‐phase techniques. The fractions which were immunoreactive in double diffusion experiments with antisera anti‐bovine and/or equine β‐lactoglobulin were subsequently purified by native PAGE and then electroblotted on Pro‐blott membrane (Western blotting). Pro‐blot membranes were stained in parallel with Coomassie and by immunostaining using antibodies against bovine and/or equine β‐lactoglobulin as first antibody solution. The immunoreactive bands were cut out from the membrane and N‐terminally sequenced; all the immunoreactive components were clearly identified as human β‐casein or its (mainly tryptic) fragments. The strong antigenic similarity between human β‐casein and β‐la...

Research paper thumbnail of Isolation of Donkey Whey Proteins and N-Terminal Amino-Acid Sequence of Alpha-Lactalbumin-A and Alpha-Lactalbumin-B, Beta-Lactoglobulin-I and Beta-Lactoglobulin-II and Lysozyme

Milchwissenschaft-milk Science International, 1989

Structures, fonctions et evolution des proteines du lactoserum de lait d'ânesse en relation a... more Structures, fonctions et evolution des proteines du lactoserum de lait d'ânesse en relation avec la genetique

Research paper thumbnail of Comparative study of casein content in human colostrum and milk

Milchwissenschaft-milk Science International, 1994

Research paper thumbnail of A pr 2 01 8 Technology networks : the autocatalytic origins of innovation

We analyse the autocatalytic structure of technological networks and evaluate its significance fo... more We analyse the autocatalytic structure of technological networks and evaluate its significance for the dynamics of innovation patenting. To this aim, we define a directed network of technological fields based on the International Patents Classification, in which a source node is connected to a receiver node via a link if patenting activity in the source field anticipates patents in the receiver field in the same region more frequently than we would expect at random. We show that the evolution of the technology network is compatible with the presence of a growing autocatalytic structure, i.e. a portion of the network in which technological fields mutually benefit from being connected to one another. We further show that technological fields in the core of the autocatalytic set display greater fitness, i.e. they tend to appear in a greater number of patents, thus suggesting the presence of positive spillovers as well as positive reinforcement. Finally, we observe that core shifts take...

Research paper thumbnail of Separation of Whey Proteins from Llama (Lama-Glama L) Milk - Identification of a Protein Immunologically Related to Beta-Lactoglobulins

Separation of llama whey proteins by size exclusion HPLC followed by purification through prepara... more Separation of llama whey proteins by size exclusion HPLC followed by purification through preparative IEF and reversed phase HPLC led to the isolation of a protein reacting with polyclonal antibody anti-bovine beta-lactoglobulin in an immuno double diffusion experiment.The N-terminal amino acid sequence of this llama whey protein showed some homology with internal parts of human k-casein and human lactotransferrin as well as an interesting identity with recognized beta-lactoglobulins in positions Pro 4 and Leu 10.

Research paper thumbnail of Isolation of donkey whey proteins and N-terminal amino acid sequence of α-lactalbumins A and B, β-lactoglobulins I and II and lyzozyme

Structures, fonctions et evolution des proteines du lactoserum de lait d'ânesse en relation a... more Structures, fonctions et evolution des proteines du lactoserum de lait d'ânesse en relation avec la genetique

Research paper thumbnail of Identification and Characterization of 2 Alpha-Lactalbumins from Somali Camel Milk (Camelus-Dromedarius)

Milchwissenschaft-milk Science International, 1985

Composition en acides amines et identification de la sequence N-terminale de deux formes d'α-... more Composition en acides amines et identification de la sequence N-terminale de deux formes d'α-lactalbumine isolees de lait de chamelle par chromatographie sur gel

Research paper thumbnail of Amino acid sequence and crystal structure of buffalo α-lactalbumin

FEBS Letters, 1996

Isolation, purification, amino acid sequence determination and X-ray crystal structure of buffalo... more Isolation, purification, amino acid sequence determination and X-ray crystal structure of buffalo alpha-lactalbumin were performed in order to gain further knowledge of the molecular basis of alpha-lactalbumin in the lactose synthase complex. The deduced amino acid sequence differs at one position from the bovine alpha-lactalbumin sequence (at position 17). The refined crystal structure at 2.3 A is very similar to those previously reported for human and baboon alpha-lactalbumins. However, a portion of the molecule (residues 105-109) exhibits different conformation. It forms a 'flexible loop', and appears to be a functionally important region in forming the lactose synthase complex.

Research paper thumbnail of Effects of two different domestic boiling practices on the allergenicity of cow's milk proteins

Journal of the Science of Food and Agriculture

Research paper thumbnail of Identification of Equine Lactadherin-Derived Peptides that Inhibit Rotavirus Infection via Integrin Receptor Competition

The Journal of biological chemistry, Jan 26, 2015

Human rotavirus is the leading cause of severe gastroenteritis in infants and children under the ... more Human rotavirus is the leading cause of severe gastroenteritis in infants and children under the age of five years in both developed and developing countries. Human lactadherin, a milk-fat globule membrane (MFGM) glycoprotein, inhibits human rotavirus infection in vitro, whereas bovine lactadherin is not active. Moreover, it protects breastfed infants against symptomatic rotavirus infections. To explore the potential antiviral activity of lactadherin sourced by equines we undertook a proteomic analysis of MFGM proteins from donkey milk and elucidated its amino acid sequence. Alignment of the human, bovine and donkey lactadherin sequences revealed the presence of an Asp-Gly-Glu (DGE) α2β1 integrin-binding motif in the N-terminal domain of donkey sequence only. Since integrin α2β1 plays a critical role during early steps of rotavirus host cell adhesion, we tested a mini-library of donkey lactadherin-derived peptides containing DGE sequence for anti-rotavirus activity. A 20 amino acid ...

Research paper thumbnail of The unusual amino acid triplet Asn-Ile-Cys is a glycosylation consensus site in human alpha-lactalbumin

Journal of protein chemistry, 1997

Human alpha-lactalbumin has not been described as a glycoprotein, despite the fact that several a... more Human alpha-lactalbumin has not been described as a glycoprotein, despite the fact that several alpha-lactalbumins of both ruminant and nonruminant species are known to be glycosylated. In all these species the glycosylation site is the 45Asn in the usual triplet 45Asn-Gly/Gln-47Ser. We have found that human alpha-lactalbumin is glycosylated and the glycosylation site has been determined by protein sequencing and mass spectrometry. We report an unusual glycosylation site at 71Asn in the triplet 71Asn-Ile-73Cys, which is conserved in all known alpha-lactalbumins except red-necked wallaby. That a relatively small proportion of the protein is glycosylated (about 1%) may reflect the importance of this region of the protein sequence to the molten globule state of alpha-lactalbumin.

Research paper thumbnail of Microanalysis of the Amino-Acid Sequence of Monomeric β-Lactoglobulin I from Donkey ( Equus asinus ) milk. The Primary Structure and its Homology with a Superfamily of Hydrophobic Molecule Transporters

Biological Chemistry Hoppe-Seyler, 1988

The complete primary structure of donkey beta-lactoglobulin I was determined by pulsed-liquid pha... more The complete primary structure of donkey beta-lactoglobulin I was determined by pulsed-liquid phase microsequencing of tryptic peptides. The protein has been isolated in monomeric form and it corresponds to monomeric beta-lactoglobulin of type I. With the inclusion of donkey beta-lactoglobulin I there are 13% common residues amongst the members of the beta-lactoglobulin family. Donkey beta-lactoglobulin I is homologous to the retinol-binding protein, bilin-binding protein and five other proteins belonging to the new superfamily of hydrophobic molecule transporters. A rapid method for peptide isolation and the strategy for microsequencing of this protein have been described.

Research paper thumbnail of The Primary Structure of Donkey (Equus asinus) Lysozyme contains the Ca(II) Binding Site of α-Lactalbumin

Biological Chemistry Hoppe-Seyler, 1988

The complete primary structure of donkey lysozyme has been established by pulsed liquid-phase seq... more The complete primary structure of donkey lysozyme has been established by pulsed liquid-phase sequencing of tryptic and chymotryptic peptides isolated by RP-HPLC. The positions of the Cys residues were identified by labeling the Cys residues with DABIA-reagent. Donkey lysozyme is a c-type lysozyme which is 129 amino acids long. It exhibits 50% homology to the human protein. We observe the full Ca(II) binding site suggested for the homologous alpha-lactalbumines. Although horse lysozyme has been reported to contain asparagine in position 61, which was in conflict with the three-dimensional structure of lysozyme, all other known c-type lysozymes, including donkey, contain Ser 61.

Research paper thumbnail of The Complete Primary Structure of α-Lactalbumin Isolated from Pig (Sus scrofa) Milk

Biological Chemistry Hoppe-Seyler, 1990

... USA 59, 491-497. Teahan, CG, McKenzie, HA & Shaw, DC (1986) llth Annual Conference on... more ... USA 59, 491-497. Teahan, CG, McKenzie, HA & Shaw, DC (1986) llth Annual Conference on Protein Structure and Function, Lome, Australia, Abstract. ... Dr. Amedeo Conti and Lorenzo Napolitano, Centro Studi Alimentazione Animali, CNR, Via P. Giuria 6.1-10125Torino, Italy. ...

Research paper thumbnail of The Complete Amino-Acid Sequence of Dimeric β-Lactoglobulin from Mouflon (Ovis ammon musimon) Milk

Biological Chemistry Hoppe-Seyler, 1987

... The Complete Amino-Acid Sequence of Dimeric /3-Lactoglobulin from Mouflon (Ovis ammon musimon... more ... The Complete Amino-Acid Sequence of Dimeric /3-Lactoglobulin from Mouflon (Ovis ammon musimon) Milk Jasminka GODOVAC-ZIMMERMANN*, Amedeo CoNTib and Lorenzo NAPOLITANO5 ... 9 Bell, K. & McKenzie, HA (1964) Nature (London) 204, 1275-1279. ...

Research paper thumbnail of Covalent Structure of the Minor Monomeric β-Lactoglobulin II Component from Donkey Milk

Biological Chemistry Hoppe-Seyler, 1990

Summary: The complete primary structure of the minor /3-lactoglobulin II component from donkey mi... more Summary: The complete primary structure of the minor /3-lactoglobulin II component from donkey milk is presented. It has been established by amino-acid sequencing and mass-spectrometry analysis of in-tact protein and peptides obtained after enzymatic and chemical ...