Leucine Aminopeptidase (Bovine Lens)
1971; Elsevier BV; Volume: 246; Issue: 8 Linguagem: Inglês
10.1016/s0021-9258(18)62309-9
ISSN1083-351X
AutoresSusanne W. Melbye, Frederick H. Carpenter,
Tópico(s)Drug Transport and Resistance Mechanisms
ResumoAbstract The stability to pH and denaturing agents of crystalline leucine aminopeptidase (bovine lens) (EC 3.4.1.1) is reported. The native enzyme exhibited a molecular weight of 327,000. In 7 m urea below pH 3 and in ≥3.7 m guanidinium chloride below pH 8.5, both leucine aminopeptidase and its reduced and carboxamidomethylated derivative exhibited a molecular weight on equilibrium centrifugation of 54,000 ± 4000 in the presence or absence of mercaptoethanol. A similar value (57,000) for the subunit of the enzyme or its carboxamidomethylated derivative was found on gel electrophoresis after incubation in 0.1 to 1.2% sodium dodecyl sulfate in the presence of mercaptoethanol.
Referência(s)