Tags

Type your tag names separated by a space and hit enter

Determination of the dissociation constants of pea diamine oxidase.
Biochem Int. 1992 Feb; 26(1):87-96.BI

Abstract

The activity of diamine oxidase [EC 1.4.3.6] (DAO) isolated from pea cotyledons was measured in Britton-Robinson buffers at pH range 5.0-9.6 by spectrophotometric method with E-1,4-diamino-2-butene as substrate. The enzyme has the highest activity at pH = 7.7 and in pH greater than 8.0 it is irreversible denaturated with time. The dissociation constants of the enzyme and enzyme-substrate complex were calculated by Dixon's method from plots of log Vmax, log KM and log Vmax/KM against pH. The pKEA = 6.5 suggests that histidine is in active site of DAO.

Authors+Show Affiliations

Pec P
Department of Analytical and Organic Chemistry, Faculty of Science, Palacký University, Czechoslovakia.
Haviger A
No affiliation info available
Frébort I
No affiliation info available

MeSH

Amine Oxidase (Copper-Containing)Binding SitesCatalaseFabaceaeHistidineHydrogen-Ion ConcentrationKineticsLiverPlants, Medicinal

Pub Type(s)

Journal Article

Language

eng

PubMed ID

1616501

Citation

Pec, P, et al. "Determination of the Dissociation Constants of Pea Diamine Oxidase." Biochemistry International, vol. 26, no. 1, 1992, pp. 87-96.
Pec P, Haviger A, Frébort I. Determination of the dissociation constants of pea diamine oxidase. Biochem Int. 1992;26(1):87-96.
Pec, P., Haviger, A., & Frébort, I. (1992). Determination of the dissociation constants of pea diamine oxidase. Biochemistry International, 26(1), 87-96.
Pec P, Haviger A, Frébort I. Determination of the Dissociation Constants of Pea Diamine Oxidase. Biochem Int. 1992;26(1):87-96. PubMed PMID: 1616501.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Determination of the dissociation constants of pea diamine oxidase. AU - Pec,P, AU - Haviger,A, AU - Frébort,I, PY - 1992/2/1/pubmed PY - 1992/2/1/medline PY - 1992/2/1/entrez SP - 87 EP - 96 JF - Biochemistry international JO - Biochem Int VL - 26 IS - 1 N2 - The activity of diamine oxidase [EC 1.4.3.6] (DAO) isolated from pea cotyledons was measured in Britton-Robinson buffers at pH range 5.0-9.6 by spectrophotometric method with E-1,4-diamino-2-butene as substrate. The enzyme has the highest activity at pH = 7.7 and in pH greater than 8.0 it is irreversible denaturated with time. The dissociation constants of the enzyme and enzyme-substrate complex were calculated by Dixon's method from plots of log Vmax, log KM and log Vmax/KM against pH. The pKEA = 6.5 suggests that histidine is in active site of DAO. SN - 0158-5231 UR - https://www.unboundmedicine.com/medline/citation/1616501/Determination_of_the_dissociation_constants_of_pea_diamine_oxidase_ DB - PRIME DP - Unbound Medicine ER -