Evidence for the presence of proteolytic activity in peroxisomes.

Abstract:

:The presence of endo- and exoproteolytic activity in peroxisomes was detected in cell organelles purified from pea leaves. By PAGE using different exopeptidase substrates (L-aa-beta NA), one leucine aminopeptidase (AP) was found in peroxisomes. The peroxisomal AP was characterized as a serine protease and had a maximal activity at pH 7.5, a molecular mass of 56.8 kDa and a pI of 5.3. This enzyme was mainly present in the soluble fraction of peroxisomes. The occurrence of proteases in peroxisomes suggests that they might be involved in the protein turnover and processing of imported precursor polypeptides in peroxisomes.

journal_name

Eur J Cell Biol

authors

Corpas FJ,Palma JM,del Río LA

subject

Has Abstract

pub_date

1993-06-01 00:00:00

pages

81-5

issue

1

eissn

0171-9335

issn

1618-1298

journal_volume

61

pub_type

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