Amino acid sequence of bovine carboxypeptidase A. Isolation and characterization of selected peptic and nagarse peptides and the complete sequence of fragment FI

Biochemistry ◽  
1971 ◽  
Vol 10 (6) ◽  
pp. 961-972 ◽  
Author(s):  
Hans Neurath ◽  
Ralph A. Bradshaw ◽  
Kenneth A. Walsh
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Complete Sequence ◽  
Carboxypeptidase A ◽  
Isolation And Characterization

Amino acid sequence of penicillopepsin. I. Isolation and characterization of the chymotryptic peptides

1976 ◽  
Vol 54 (10) ◽  
pp. 872-884 ◽  
Author(s):  
Alexander Kurosky ◽  
Theo Hofmann
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
Acid Protease ◽  
Terminal Region ◽  
Isolation And Characterization

The amino acid sequences of 48 peptides obtained from a chymotryptic digest of the mould acid protease, penicillopepsin (EC 3.4.23.7), have been determined. These peptides established the sequences of 26 unique fragments of up to 28 residues in length. The 28-residue fragment was identified as the N-terminal region. The C-terminal region is represented by a 13-residue fragment. The amino acids contained in these fragments account for some 85% of the residues of the enzyme.

Isolation and characterization of two new N-glycosidase type-1 ribosome-inactivating proteins, unrelated in amino-acid sequence, from Petrocoptis species

Planta ◽  
1994 ◽  
Vol 194 (4) ◽  
pp. 487-491 ◽  
Author(s):  
F. Javier Arias ◽  
M. Angeles Rojo ◽  
J. Miguel Ferreras ◽  
Rosario Iglesias ◽  
Raquel Muñoz ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Ribosome Inactivating Proteins ◽  
Isolation And Characterization

The isolation and characterization of a new form of porcine pancreatic carboxypeptidase A (carboxypeptidase Ae)

1970 ◽  
Vol 48 (1) ◽  
pp. 7-11 ◽  
Author(s):  
A. Sampath Narayanan ◽  
R. A. Anwar
Keyword(s):  
Amino Acid ◽  
Genetic Variants ◽  
Gel Electrophoresis ◽  
Enzyme Preparation ◽  
Zinc Content ◽  
Sedimentation Equilibrium ◽  
Carboxypeptidase A ◽  
Isolation And Characterization ◽  
New Form

A new porcine carboxypeptidase A, designated as Ae, has been isolated from twice crystallized elastase. The enzyme preparation appeared homogeneous in the ultracentrifuge and gel electrophoresis, and had an s20,w of 3.34 S. A molecular weight of 34 700 was obtained from sedimentation equilibrium and the zinc content was 0.93 mole/mole enzyme. The new enzyme differs from the known porcine carboxy-peptidases (Aj, A2, A3) in solubility properties and amino acid composition. The amino acid compositions of Ai, A2, and Ae, which mainly differ in the content of isoleucine, are suggestive of their being genetic variants due to several amino acid replacements in the molecule.

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