CRYSTALLINE PAPAIN
نویسندگان
چکیده
منابع مشابه
Crystalline Papain.
In an earlier study (1) of the amino acid composition of papain, it was assumed that all of the sulfur could be attributed to cysteine and cystine since methionine is absent from this protein. However, because of the sulfhydryl nature of this enzyme, the content of these amino acids is of some importance; we have used the method of Schram, Moore, and Bigwood (2) for this estimation. The results...
متن کاملISOLATION AND PROPERTIES OF CRYSTALLINE pAPAIN*
Proteolytic enzymes from plant tissues have in general resisted purification more successfully than those of animal origin. Proteinases have been extracted from many plants, among them yeast (9), pineapple (27), pumpkin (27), beans,’ and wheat (4), but much concentration and purification are usually required before a preparation of even moderate activity is obtained. This presents difficulties ...
متن کاملThe effect of urea and guanidine hydrochloride on activity and optical rotation of crystalline papain.
The catalytic activity of several proteolytic enzymes is altered by high concentrations of urea and guanidine salts (2-4). These studies, in conjunction with certain physical data, indicate that hydrogen bonding in the secondary structure of these enzymes is essential for maintenance of their catalytic function. Because of the increasing amount of information that is available concerning the st...
متن کاملThe Digestion and Inactivation of Crystalline Urease by Pepsin and by Papain
The identity of the enzyme urease with the octahedral globulin crystals isolated by the senior author from the jack bean in 1926 (1) has been challenged by Waldschmidt-Leitz and Steigerwaldt (2). These investigators published a paper in which they claimed that crystalline urease is not inactivated at pH 7.0 by incubation with trypsin or papain, while the protein component of the urease undergoe...
متن کاملThe Catalytic Effect of Active Crystalline Papain on the Denaturation of Thyroglobulin*
It has been assumed that denaturation occurs preliminary to enzymatic hydrolytic fission in some proteins. The basis of this supposition is the generally accepted observation that these proteins arc less readily attacked by proteolytic enzymes in their native state than when they are denatured (l-3). In the case of such readily digestible proteins as gelatin, prolamin, or casein, Linderstrom-La...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1954
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)65669-8