منابع مشابه
The Milk-clotting Action of Papain*
Although the milk-clotting action of papain has been recognized for many years, this property of the enzyme has received little quantitative attention. It appears to be, however, a characteristic property of the proteolytic component of this enzyme system. Various workers have brought forth evidence as to the composite nature of the papain system, which has at least two components. In the most ...
متن کاملClotting of mammalian fibrinogens by papain: a re-examination.
Papain has long been known to cause the gelation of mammalian fibrinogens. It has also been reported that papain-fibrin is insoluble in dispersing solvents like strong urea or sodium bromide solutions, similar to what is observed with thrombin-generated clots in the presence of factor XIIIa and calcium. In those old studies, both the gelation and subsequent clot stabilization were attributed to...
متن کاملMilk-clotting Enzymes from Microorganisms.
A total of 230 cultures of fungi and 43 cultures of bacteria, isolated from such sources as soil, butter, and milk, were screened for their milk-clotting activity. The fungi were cultivated on semisolid media, and the bacteria were grown in milk media in shake culture. Phytic acid, added as calcium phytate, was found to stimulate production of the enzyme in most of the bacterial isolates. Prote...
متن کاملThe clotting action of Russell viper venom.
By SAMUEL I. RAPAPORT, KNIJT AAS ANI) PAUL A. OWREN T HE DE1\IONSTRATION of the thromboplastin-hike activity of Russell viper venom by Macfarlane and Barnett’ was followed by its use in some laboratories as a substitute for brain thromboplastin in “prothrombin time” determinations. However, it gradually became apparemit that there were importamit differences between the ‘thromboplastic” activit...
متن کاملAction of papain on human serum globulins.
Studies on the degradation of animal and human serum antibody type proteins by various proteolytic enzymes have indicated that molecules of approximately one-half and one-quarter the size of the parent 160,000-molecular weight protein may be readily formed (l-5). Porter (6) has recently shown that rabbit y-globulin is degraded by papain into fragments of the above size range and has separated s...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1937
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)74304-4