Tags

Type your tag names separated by a space and hit enter

Subunit constitution of electrophoretically purified xanthine dehydrogenase of avian liver.
J Biochem. 1984 Feb; 95(2):405-12.JB

Abstract

Chick liver xanthine dehydrogenase was highly purified by preparative polyacrylamide gel electrophoresis at the final step of purification, which allowed removal of another contaminating, xanthine-oxidizing enzyme showing a molecular mass of about 380K daltons. Purified XDH showed a specific activity higher than 2,500 units per mg of protein. On treatment with sodium dodecyl sulfate and 2-mercapto-ethanol, XDH was split into two subunits (named as alpha and beta) of different size in an equimolar ratio. The molecular weights of these subunits were estimated as 155K for alpha and 135K for beta. In the form of sodium dodecyl sulfate-complex, subunit alpha tended to degrade into smaller peptides, whereas subunit beta was relatively stable.

Authors

No affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

6585363

Citation

Irie, S. "Subunit Constitution of Electrophoretically Purified Xanthine Dehydrogenase of Avian Liver." Journal of Biochemistry, vol. 95, no. 2, 1984, pp. 405-12.
Irie S. Subunit constitution of electrophoretically purified xanthine dehydrogenase of avian liver. J Biochem. 1984;95(2):405-12.
Irie, S. (1984). Subunit constitution of electrophoretically purified xanthine dehydrogenase of avian liver. Journal of Biochemistry, 95(2), 405-12.
Irie S. Subunit Constitution of Electrophoretically Purified Xanthine Dehydrogenase of Avian Liver. J Biochem. 1984;95(2):405-12. PubMed PMID: 6585363.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Subunit constitution of electrophoretically purified xanthine dehydrogenase of avian liver. A1 - Irie,S, PY - 1984/2/1/pubmed PY - 1984/2/1/medline PY - 1984/2/1/entrez SP - 405 EP - 12 JF - Journal of biochemistry JO - J Biochem VL - 95 IS - 2 N2 - Chick liver xanthine dehydrogenase was highly purified by preparative polyacrylamide gel electrophoresis at the final step of purification, which allowed removal of another contaminating, xanthine-oxidizing enzyme showing a molecular mass of about 380K daltons. Purified XDH showed a specific activity higher than 2,500 units per mg of protein. On treatment with sodium dodecyl sulfate and 2-mercapto-ethanol, XDH was split into two subunits (named as alpha and beta) of different size in an equimolar ratio. The molecular weights of these subunits were estimated as 155K for alpha and 135K for beta. In the form of sodium dodecyl sulfate-complex, subunit alpha tended to degrade into smaller peptides, whereas subunit beta was relatively stable. SN - 0021-924X UR - https://www.unboundmedicine.com/medline/citation/6585363/Subunit_constitution_of_electrophoretically_purified_xanthine_dehydrogenase_of_avian_liver_ L2 - https://joi.jlc.jst.go.jp/JST.Journalarchive/biochemistry1922/95.405?lang=en&from=PubMed DB - PRIME DP - Unbound Medicine ER -