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Purification and properties of xanthine dehydrogenase from Pseudomonas acidovorans.
Biochim Biophys Acta. 1975 Nov 20; 410(1):12-20.BB

Abstract

Xanthine dehydrogenase (EC 1.2.1.37) from Pseudomonas acidovorans has been purified to near homogeneity (approx. 65-fold). The enzyme has a molecular weight of about 275 000. Electrophoresis in gels containing sodium dodecyl sulphate showed the presence of two types of subunit with molecular weights of about 81 000 and 63 000. Thus the intact molecule probably contains two of each type of subunit. Xanthine and hypoxanthine are good substrates, and NAD+ is an effective electron acceptor. With xanthine and NAD+ as substrates the purified enzyme has a specific activity of about 20 mumol NADH formed/min per mg protein. Michaelis constants for xanthine and NAD+ are 0.07 and 0.12 mM, respectively, and for hypoxanthine and NAD+ 0.29 and 0.16 mM, respectively.

Authors

No affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

1191668

Citation

Sin, I L.. "Purification and Properties of Xanthine Dehydrogenase From Pseudomonas Acidovorans." Biochimica Et Biophysica Acta, vol. 410, no. 1, 1975, pp. 12-20.
Sin IL. Purification and properties of xanthine dehydrogenase from Pseudomonas acidovorans. Biochim Biophys Acta. 1975;410(1):12-20.
Sin, I. L. (1975). Purification and properties of xanthine dehydrogenase from Pseudomonas acidovorans. Biochimica Et Biophysica Acta, 410(1), 12-20.
Sin IL. Purification and Properties of Xanthine Dehydrogenase From Pseudomonas Acidovorans. Biochim Biophys Acta. 1975 Nov 20;410(1):12-20. PubMed PMID: 1191668.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification and properties of xanthine dehydrogenase from Pseudomonas acidovorans. A1 - Sin,I L, PY - 1975/11/20/pubmed PY - 1975/11/20/medline PY - 1975/11/20/entrez SP - 12 EP - 20 JF - Biochimica et biophysica acta JO - Biochim Biophys Acta VL - 410 IS - 1 N2 - Xanthine dehydrogenase (EC 1.2.1.37) from Pseudomonas acidovorans has been purified to near homogeneity (approx. 65-fold). The enzyme has a molecular weight of about 275 000. Electrophoresis in gels containing sodium dodecyl sulphate showed the presence of two types of subunit with molecular weights of about 81 000 and 63 000. Thus the intact molecule probably contains two of each type of subunit. Xanthine and hypoxanthine are good substrates, and NAD+ is an effective electron acceptor. With xanthine and NAD+ as substrates the purified enzyme has a specific activity of about 20 mumol NADH formed/min per mg protein. Michaelis constants for xanthine and NAD+ are 0.07 and 0.12 mM, respectively, and for hypoxanthine and NAD+ 0.29 and 0.16 mM, respectively. SN - 0006-3002 UR - https://www.unboundmedicine.com/medline/citation/1191668/Purification_and_properties_of_xanthine_dehydrogenase_from_Pseudomonas_acidovorans_ L2 - https://linkinghub.elsevier.com/retrieve/pii/0005-2744(75)90203-X DB - PRIME DP - Unbound Medicine ER -