Bishnu Sanwal - Academia.edu (original) (raw)

Papers by Bishnu Sanwal

Proceedings / Indian Academy of Sciences

Journal of Biological Chemistry

Membrane vesicles prepared from a strain of Escherichia coli which lacks membrane-bound succinate... more Membrane vesicles prepared from a strain of Escherichia coli which lacks membrane-bound succinate dehydrogenase and fumarate reductase activity are capable of accumulating succinate in the presence of D(-)lactate or reduced phenazine methosulfate as electron donors.

Cover title. "Veröffentlicht in 'Phytopathologische Zeitschrift', Band 25, Heft 4 (1... more Cover title. "Veröffentlicht in 'Phytopathologische Zeitschrift', Band 25, Heft 4 (1956)." Thesis (Ph. D.)--Swiss Federal Institute of Technology, Zurich. Vita. Bibliography: p. 380-384.

Somatic Cell Genetics, 1976

Hybrids obtained from crosses of rat myoblasts and mouse L-cells are unable to differentiate into... more Hybrids obtained from crosses of rat myoblasts and mouse L-cells are unable to differentiate into myotubes. The synthesis of muscle-specific proteins, creatine phosphokinase (CPK), myosin, and adenyl cyclase is also suppressed in the hybrids. Adenyl cyclase produced in the hybrids is not activated by isoproterenol. The glycine auxotrophy of myoblasts is pheno!ypically expressed as a dominant trait in hybrids. Genotypically, however, all the enzymes of the phosphorylated pathway of serine biosynthesis and serine hydroxymethyltransferase, the enzyme interconverting serine and glycine, are present in normal concentrations in the hybrids, just as they are in the mouse L-cells. Unlike either of the parental lines, the hybrid cells are unable to grow on serine-supplemented medium, but do so when glycine is also added. Glycine by itself supports growth of the hybrids in the absence of added serine. All the curious effects of glycine/serine on growth of hybrids are rationalized and accounted for by the hypothesis that in these cells the enzyme serine hydroxymethyltransferase, for unknown reasons, does not function in vivo.

The Journal of biological chemistry, Jan 25, 1984

From a highly myogenic permanent line of rat skel-myoblasts (L6), we have isolated two classes of... more From a highly myogenic permanent line of rat skel-myoblasts (L6), we have isolated two classes of single step concanavalin A-resistant mutants. The RI class is about 2-fold and RII about 5-fold more resistant than the parental cells to the lethal action of concanavalin A. In all of the mutants, both the morphological differentiation (i.e. fusion to form myotubes) and biochemical differentiation, measured by the appearance of creatine kinase and acetylcholine receptors, are absent. The biochemical lesion in the RI type of mutants is not known, but RII type of mutants is unable to catalyze transfer of mannose from GDP-mannose into a lipid-linked form. Concanavalin A binding to separated membrane proteins from RII type of mutants on polyacrylamide gels is reduced 80% compared to wild type cells. In the RI type of mutants, however, only one major band, approximately 46,000 daltons, does not bind concanavalin A to the same extent as the wild type cells. In somatic cell hybridizations, RI...

The Biochemical journal, 1972

The Journal of biological chemistry, Jan 10, 1974

Reprint requests may be sent to this address. suits in changing the conformation of the protein t... more Reprint requests may be sent to this address. suits in changing the conformation of the protein to a low affinity state for aspartate. We have been interested for some time (see review, Ref. 1) in the nature and mechanism of control of the enzymes of amphibolic pathways in bacteria. One of the important enzymes of this pathway in the enteric bacteria is phosphoenolpyruvate carbosylase (EC 4.1.1.31)) and it has been demonstrated earlier in the case of Salmonella typhimurium that the enzyme is inhibited by L-aspartate (2) and activated by several phosphorylated compounds such as acetyl coenzyme A (3), fructose 1 ,6-diphosphate (4), and guanosine triphosphate (5). In addition, some organic solvents, such as ethanol and dioxane, and some highly charged polyamino acids (6) powerfully activate the enzyme and in some cases desensitize it to feedback inhibitors. P-enolpyruvate carboxylase from another enteric bacterium, Escherichia

The Journal of biological chemistry, Jan 15, 1991

Several cDNA clones encoding a 46-kDa collagen-binding glycoprotein (gp46) from rat skeletal myob... more Several cDNA clones encoding a 46-kDa collagen-binding glycoprotein (gp46) from rat skeletal myoblasts were isolated and sequenced. The cDNA encoded a 17-amino acid signal peptide and a 400-amino acid mature protein, containing three potential N-linked oligosaccharide attachment sites. The cDNA sequence of gp46 shows 93% identity in the coding region with J6, a retinoic acid-inducible gene coding for a protein of unknown function described from embryonal carcinoma F9 cells. The first 41 NH2-terminal amino acids of the predicted J6 sequence are, however, different from the gp46 sequence as a result of a 7-base pair insertion in the gp46 cDNA. In addition, the NH2-terminal amino acid sequence of hsp47, a collagen-binding protein found in chick embryo fibroblasts, shows 64% identity to gp46 over 36 residues. Interestingly, this alignment begins 10 residues inward from the first amino acid in the mature form of gp46. A significant sequence similarity was observed between gp46 and member...

Somatic cell genetics, 1978

In rat skeletal myoblasts which are resistant to 5-azacytidine and fusion-incompetent, the muscle... more In rat skeletal myoblasts which are resistant to 5-azacytidine and fusion-incompetent, the muscle-specific protein, creatine phosphokinase, is produced but muscle-specific myosin is not. In human diploid fibroblast X rat myoblast hybrids, myoblast-specific properties are extinguished. Clones can be selected from the hybrids after a number of doublings which reexpress fusion but do not produce creatine phosphokinase. The conclusion is drawn that the expression of muscle-specific phenotype is not coordinate and fusion of myoblasts is not an essential requirement for the appearance of myoblast-specific proteins.

The Journal of biological chemistry, Jan 10, 1979

Biochimica et biophysica acta, 1965

Advances in experimental medicine and biology, 1997

Colligin is a major glycoprotein in many cells and has been discovered several times by different... more Colligin is a major glycoprotein in many cells and has been discovered several times by different approaches and hence given different names. Kurkinen et al. (1984) first found it as a collagen-binding protein in parietal endoderm cells and proposed the name‘colligin’ but it was later detected as a differentiation related protein in myoblasts (‘gp46’) (Cates et al., 1984) and as a heat shock responsive protein in chick fibroblasts (HSP47) (Nagata & Yamada, 1986). Sequencing later confirmed the identity of the various proteins. Each of the routes of discovery delivered clues about the function of the protein, leading eventually to the current idea of a role as a molecular chaperone in collagen synthesis.

The Journal of biological chemistry, Jan 25, 1994

We have been studying cAMP signaling in L6 myoblasts because of its potential role in regulating ... more We have been studying cAMP signaling in L6 myoblasts because of its potential role in regulating the differentiation of these cells into multinucleate myotubes. Previous studies have shown that treatment of L6 myoblasts with cAMP analogs causes an increase in cAMP phosphodiesterase activity. To assess the role of protein kinase A in this cAMP-mediated increase in cAMP phosphodiesterase activity, L6 myoblasts were transfected with a plasmid containing the cDNA for a mutant regulatory subunit of protein kinase A, which functions as a dominant negative inhibitor of this enzyme. The cDNA was under control of the metallothionein promoter in the construct. Induction of the mutant regulatory subunit with Zn2+ decreased cAMP-dependent protein kinase activity by 90%. Zn2+ treatment was also able to completely block the cAMP-mediated increase in phosphodiesterase activity, showing that this effect is mediated by protein kinase A. The activity of the cAMP-induced phosphodiesterase was inhibite...

Journal of bacteriology, 1981

A mutation has been characterized in Escherichia coli which results in temperature-sensitive expr... more A mutation has been characterized in Escherichia coli which results in temperature-sensitive expression of phosphoenolpyruvate carboxykinase activity and antigen. The enzyme produced by the mutant strain at a permissive temperature or by cells treated with chloramphenicol at nonpermissive temperatures had normal activity and stability in extracts. Since phosphoenolpyruvate carboxykinase had a monomeric structure, the mutation probably affects the synthesis, rather than the structure or assembly, of the enzyme.