Isolation and characterization of a complementary DNA clone coding for the E1.beta. subunit of the bovine branched-chain .alpha.-ketoacid dehydrogenase complex: complete amino acid sequence of the precursor protein and its proteolytic processing

Biochemistry ◽  
1990 ◽  
Vol 29 (5) ◽  
pp. 1154-1160 ◽  
Author(s):  
Yoshitaka Nobukuni ◽  
Hiroshi Mitsubuchi ◽  
Fumio Endo ◽  
Junichiro Asaka ◽  
Rieko Oyama ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Proteolytic Processing ◽  
Beta Subunit ◽  
Complementary Dna ◽  
Isolation And Characterization ◽  
Branched Chain ◽  
Ketoacid Dehydrogenase ◽  
Dehydrogenase Complex

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.

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