Affiliation:
1. Department of Biochemistry, The Graduate School and the Stritch School of Medicine, Loyola University, Chicago, Ill
Abstract
Abstract
Using the combined technics of the ionographic separation of serum proteins in a paper-stabilized medium, as described by McDonald et al. (16, 17, 18), and the spectrophotometric procedure for the determination of transaminase activity developed by Karmen (3, 14), the electrophoretic migration pattern of the enzyme glutamic oxalacetic transaminase in rat serum has been examined. The major portion of the transaminase activity has been found to be associated with the α-2 globulin fraction of the serum proteins. Further evidence has been presented for the assumption of a nonionic linkage between the enzyme and its coenzyme, pyridoxal phosphate.
Publisher
Oxford University Press (OUP)
Subject
Biochemistry (medical),Clinical Biochemistry
Cited by
8 articles.
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