Disulfide bridges of bovine spleen cathepsin B. [Biol Chem Hoppe Seyler. 1990]

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1: Biol Chem Hoppe Seyler. 1990 Jun;371(6):485-91.Links

Disulfide bridges of bovine spleen cathepsin B.

Baudys M, Meloun B, Gan-Erdene T, Pohl J, Kostka V.

Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Sciences, Prague, CSFR.

Bovine spleen cathepsin B contains 7 disulfide bridges. Cleavage of the enzyme with cyanogen bromide gives rise to a large and a small fragment. The former contains all disulfide bridges. Their arrangement was determined by analysis of amino-acid sequences and compositions of subfragments prepared by cleavage of the large cyanogen-bromide fragment with trypsin, chymotrypsin and the staphylococcal proteinase using specific methods for the detection of S-S-bonds. Disulfide bridges link together Cys14-Cys43, Cys26-Cys71, Cys62-Cys128, Cys63-Cys67, Cys100-Cys132, Cys108-Cys119 and Cys148-Cys252.

PMID: 2390214 [PubMed - indexed for MEDLINE]

S-S bridges of cathepsin B and H from bovine spleen: a basis for cathepsin B model building and possible functional implications for discrimination between exo- and endopeptidase activities among cathepsins B, H and L.
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[Biomed Biochim Acta. 1991]
Identification of the second (buried) cysteine residue and of the C-terminal disulfide bridge of bovine spleen cathepsin B.
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[Biol Chem Hoppe Seyler. 1988]
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Cited by 2 PubMed Central articles

Demonstration by electrospray mass spectrometry that the peptidyldipeptidase activity of cathepsin B is capable of rat cathepsin B C-terminal processing.
Rowan AD, Feng R, Konishi Y, Mort JS. Biochem J. 1993 Sep 15; 294 ( Pt 3):923-7.

[Biochem J. 1993]
The refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity.
Musil D, Zucic D, Turk D, Engh RA, Mayr I, Huber R, Popovic T, Turk V, Towatari T, Katunuma N. EMBO J. 1991 Sep; 10(9):2321-30.

[EMBO J. 1991]

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