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Biochem Biophys Res Commun. 1996 Nov 12;228(2):341-6.

In vitro association with peroxisomes and conformational change of peroxisomal serine:pyruvate/alanine:glyoxylate aminotransferase in rat and human livers.

Author information

1
Department of Biochemistry, Hamamatsu University School of Medicine, Shizuoka, Japan. odat129@hama-med.ac.jp

Abstract

To understand the targeting mechanisms of peroxisomal serine:pyruvate aminotransferase, in vitro import experiments were carried out using this 43 kDa peroxisomal enzyme, which was synthesized in a coupled transcription/translation system. Being different from other peroxisomal enzymes, such as acyl-CoA oxidase and urate oxidase used in previous in vitro import experiment, the soluble form of peroxisomal serine:pyruvate aminotransferase was fairly resistant to proteinase K digestion. However, the enzyme recovered in the peroxisomal fraction was proteinase K sensitive. This indicates that the association of peroxisomal serine:pyruvate aminotransferase with the peroxisomal membrane causes a marked conformational change in the structure of this protein.

PMID:
8920916
DOI:
10.1006/bbrc.1996.1663
[Indexed for MEDLINE]

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