Acta biologica et medica Germanica.
Discontinued
Publisher:
Akademie Verlag
Frequency: Monthly
Country: Germany
Language: ger
Start Year:1958 - 1982
Identifiers
| ISSN: | 0001-5318 (Print) 0001-5318 (Linking) |
| NLM ID: | 0370276 |
| (DNLM): | A04500000(s) |
| (OCoLC): | 01460849 |
| Coden: | ABMGAJ |
| Classification: | W1 AC763 |
Cibacron Blue-induced modification of neutral proteinase from horse blood leukocytes. The proteolytic activity of the elastase-like proteinase from granules of horse blood leukocytes is retained on a column of Cibacron Blue-Sepharose and can be eluted with 0.5 M KSCN. During this procedure its mol. wt. is reduced from 49000 to 30000 and isoelectric point is shifted towards higher pH. The inactive protein not adsorbed on Cibacron Blue-Sepharose is strongly acidic and shows a mol. wt. of 20000. Upon mixing this protein with the modified enzyme the native proteinase is reconstituted as shown by polyacrylamide gel electrophoresis at pH 8.3 and isoelectric focusing in a sucrose grad...
[Effect of low pH values on the infectivity and neuraminidase activity of human and animal strains of influenza virus type A]. The influence of acidic pH on the infectivity and neuraminidase activity of human, equine and avian type A influenza virus strains has been studied. Following exposure to pH 3 human and equine strains lost their infectivity completely, whereas all investigated strains of the subtypes Hav6N2 and Hav7Neq2 retained a certain amount of infectivity. In contrast to human and equine strains the avian strains retained also 38% of their original neuraminidase activity after acidic treatment. Partial retention of infectivity and the relative stability of the neuraminidase following exposure to acidic pH...
Interaction of horse plasma antithrombin III and alpha 1-proteinase inhibitor with some serine proteinases. Antithrombin III and alpha 1-proteinase inhibitor isolated simultaneously from horse citrated plasma were tested for inhibitory activity against bovine trypsin and chymotrypsin, as well as elastase-like neutral proteinases from horse leucocytes. The stoichiometry of reaction and kinetic parameters (kass, Ko) were estimated and related to the protein pattern obtained after exposure of these proteinases to horse inhibitors as analyzed by polyacrylamide gel electrophoresis (PAGE and PAGE-SDS). As shown by fast reaction rates and low values of dissociation constants the two inhibitors effectively ...