Primary Structure of Bovine Carboxypeptidase B
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 کاملIdentification of a glutamic acid at the active center of bovine carboxypeptidase B.
The glutamic acid residue at the active center of bovine carboxypeptidase B was labeled with a-N-bromoacetyl-D[5J4C]arginine and the alkylated protein was hydrolyzed with pepsin. A 14C-labeled peptide fraction was isolated in a 52% yield by gel filtration on Sephadex G-25 followed by ion exchange chromatography on CM-cellulose. Compositional and end group analysis, in addition to enzymatic hydr...
متن کاملEvidence for a carboxyl group at the active center of bovine carboxypeptidase B.
Bovine carboxypeptidase B has been alkylated at the active center by or-N-bromoacetyl-D-arginine-5-14C. The enzyme was treated at pH 7.0 with a 40-fold molar excess of the reagent. Subsequent fractionation of the reaction mixture on Sephadex G-25 and L-leucyl-D-arginine-Sepharose 4B columns has shown that inactivation is accompanied by incorporation of 1.09 moles of alkylating agent per mole of...
متن کاملDynamical structure of carboxypeptidase A.
Structural fluctuations of the apoenzyme form of carboxypeptidase A (EC 3.4.12.2) have been evaluated on the basis of molecular dynamics. The Konnert-Hendrickson refined coordinates of 2437 non-hydrogen atoms of the 307 amino acid residues derived from the X-ray structure of the holoenzyme served as the molecular model together with 548 calculated polar hydrogen atoms and 25 buried solvent mole...
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...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1974
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)42538-6