Bovine carboxypeptidase A variants resulting from allelomorphism.
نویسندگان
چکیده
منابع مشابه
New forms of bovine carboxypeptidase B and their homologous relationships to carboxypeptidase A.
Two new forms of carboxypeptidase B have been isolated from spontaneously activated bovine pancreatic juice. The fully active enzymes contain an internal split at residues 92-93 and 95-96, respectively. Sequenator analysis of the amino terminal segments of the two chains of the enzyme has extended the sequence information by 51 amino acid residues. Comparison of 125 residues strengthens the hyp...
متن کاملThe amino acid sequence of bovine carboxypeptidase A. 3.
The amino acid sequence of the four fragments produced by treatment of bovine carboxypeptidase A with cyanogen bromide has been completed. The alignment of these fragments, previously established by peptic digest of the whole protein, allows for the description of the complete primary structure of the molecule. A comparison of the proposed functional residues, identified by X-ray diffraction an...
متن کاملCarboxypeptidase from Yeast
In order to render the carboxypeptidase from yeast more readily available for use in sequence studies in protein chemistry, the procedure of Hata, Hayashi, and associates for the preparation of the enzyme has been adapted to a larger scale through cooperation with the New England Enzyme Center. From 100 pounds of bakers’ yeast, the yield was about 1.4 g of the chromatographically purified, elec...
متن کاملCarboxypeptidase A
Scientific and technological advances brought about in the recent part of this decade have provided great insight regarding the catalytic mechanism of the prototypical zinc-requiring protease carboxypeptidase A (CPA). Importantly, some of our ideas regarding the general theory of enzyme catalysis have been inspired and developed through studies of this enzyme. Just as importantly, CPA serves as...
متن کاملCharacterisation of a carboxypeptidase in human serum distinct from carboxypeptidase N.
Arginine carboxypeptidase activity in human serum, measured with the hippuryl-L-arginine substrate, is about three times higher than in human plasma. This difference is much smaller when hippuryl-L-lysine is used as the substrate. When fresh serum is incubated at 30 degrees C, the arginine and lysine carboxypeptidase activity decreases until a stable activity, close to the plasma activity, is r...
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: Proceedings of the National Academy of Sciences
سال: 1966
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.56.4.1339