Porcine Spleen Deoxyribonuclease II
نویسندگان
چکیده
منابع مشابه
Porcine Spleen Deoxyribonuclease II
Porcine spleen DNase II, a lysosomal acid hydrolase, is a noncovalently linked azb heterodimer (Liao, T.-H. (1985) J. Biol. Chem. 260, 10708–10713). The a subunit, after disulfide cleavage, yields two chains, a1 and a2. The complete amino acid sequences of the a1, b, and a2 chains were elucidated by protein sequencing, and the pairings of one interchain disulfide between a1 and a2 and of three ...
متن کاملThe subunit structure and active site sequence of porcine spleen deoxyribonuclease.
An acid DNase (DNase II) from porcine spleen was purified by sequential chromatography over carboxymethyl-cellulose, blue dextran-Sepharose, hydroxylapatite, and sulfoxyethyl-cellulose. The purified enzyme shows two polypeptide bands on sodium dodecyl sulfate-polyacrylamide gel electrophoresis at Mr 35,000 (alpha chain) and 10,000 (beta chain). The sum of the two molecular weights is that of th...
متن کاملThe separation of the phosphodiesterase and deoxyribonuclease II activities of bovine spleen.
Deoxyribonuclease II (Deoxyribonucleate 3’-nucleotidohydrolase, EC 3.1.4.6) was purified 1250-fold from bovine spleen. The specific activity of the final preparation was 408. It was free of phosphatase and alkaline ribonuclease, and almost free of nonspecific phosphodiesterase, acid ribonuclease, and adenosine triphosphatase. Chromatography on carboxymethyl cellulose prior to heating caused the...
متن کاملPorcine spleen cathepsin B is an exopeptidase.
The major cathepsin B isozyme CB-I purified from porcine spleens was studied for its specificity against various peptide and denatured protein substrates. The enzyme degraded all the peptide substrates by an exopeptidase activity. The substrates were degraded mainly by a dipeptidyl carboxypeptidase activity of the enzyme except for angiotensin I, from which a COOH-terminal leucine residue was r...
متن کاملIdentification of deoxyribonuclease II as an endonuclease involved in apoptosis.
Cell death occurs by apoptosis during programmed deletion of cells and following exposure to cytotoxic agents. Central to the mechanism of apoptosis is internucleosomal DNA digestion by an endogenous endonuclease which is thought to mediate cell death. An axiom of apoptosis is that the endonuclease involved is a Ca2+/Mg(2+)-dependent endonuclease. During purification of endonucleases from Chine...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1998
ISSN: 0021-9258
DOI: 10.1074/jbc.273.27.17192