Hannah Ochim - Academia.edu (original) (raw)
Uploads
Papers by Hannah Ochim
... Jean Harlow 62 Sophia Loren 92 Der blonde Leinwandstar der 1930-er Jahre Der italienische Fil... more ... Jean Harlow 62 Sophia Loren 92 Der blonde Leinwandstar der 1930-er Jahre Der italienische Filmstar der 1960-er Jahre Rita Hayworth 65 Anna Magnani 95 Die „Venus Die „Urmutter des Atomzeitalters“ des italienischen Films“ Katharine Hepburn 68 Guiletta Masina 97 Die ...
Biochimica et Biophysica Acta (BBA)-Lipids and Lipid …, 1970
Biochimica et biophysica acta, 1963
Several enzyme and other fractions of venoms were studied to determine the component (or componen... more Several enzyme and other fractions of venoms were studied to determine the component (or components) responsible for rendering axonal conduction sensitive to the action of acetylcholine and curare. A phosphollpase A (EC 3.1.1.4)-rich fraction from cobra venom and phospholipase D (EC 3.I.4.4) rendered the squid axon sensitive to the action of curare. Venom phosphodiesterase (EC 3.I.4.1), apparently also active, was found to have considerable phospholipase A activity. A phospholipase A-poor fraction of cobra venom, L-amino acid oxidase (EC 1.4.3.z ), Cobroxin, lysolecithin and phospholipase C (EC 3.I.4.3) were all ineffective in rendering curare active on the squid axon. All the enzymes and venom products tested were relatively weak in their direct effects on conduction except for the phospholipase A-rich fraction. Heating a solution of cottonmouth venom at an alkaline pH destroyed almost all o~ its phospholipase A activity whereas heating at an acid pH had little effect on this enzymic activity. Eastern diamondback rattlesnake venom hydrolyzes egg lecithin at a rate only slightly less than that of cottonmouth venom. The ability of several venoms to hydrolyze beef lecithin was also compared. The results support the assumption that the phospholipase A of venoms is responsible for their ability to increase the permeability of the squid axon allowing thereby acetylcholine and curare to penetrate into the axon and to affect conduction.
... Jean Harlow 62 Sophia Loren 92 Der blonde Leinwandstar der 1930-er Jahre Der italienische Fil... more ... Jean Harlow 62 Sophia Loren 92 Der blonde Leinwandstar der 1930-er Jahre Der italienische Filmstar der 1960-er Jahre Rita Hayworth 65 Anna Magnani 95 Die „Venus Die „Urmutter des Atomzeitalters“ des italienischen Films“ Katharine Hepburn 68 Guiletta Masina 97 Die ...
Biochimica et Biophysica Acta (BBA)-Lipids and Lipid …, 1970
Biochimica et biophysica acta, 1963
Several enzyme and other fractions of venoms were studied to determine the component (or componen... more Several enzyme and other fractions of venoms were studied to determine the component (or components) responsible for rendering axonal conduction sensitive to the action of acetylcholine and curare. A phosphollpase A (EC 3.1.1.4)-rich fraction from cobra venom and phospholipase D (EC 3.I.4.4) rendered the squid axon sensitive to the action of curare. Venom phosphodiesterase (EC 3.I.4.1), apparently also active, was found to have considerable phospholipase A activity. A phospholipase A-poor fraction of cobra venom, L-amino acid oxidase (EC 1.4.3.z ), Cobroxin, lysolecithin and phospholipase C (EC 3.I.4.3) were all ineffective in rendering curare active on the squid axon. All the enzymes and venom products tested were relatively weak in their direct effects on conduction except for the phospholipase A-rich fraction. Heating a solution of cottonmouth venom at an alkaline pH destroyed almost all o~ its phospholipase A activity whereas heating at an acid pH had little effect on this enzymic activity. Eastern diamondback rattlesnake venom hydrolyzes egg lecithin at a rate only slightly less than that of cottonmouth venom. The ability of several venoms to hydrolyze beef lecithin was also compared. The results support the assumption that the phospholipase A of venoms is responsible for their ability to increase the permeability of the squid axon allowing thereby acetylcholine and curare to penetrate into the axon and to affect conduction.