| Literature DB >> 3693402 |
T Imanaka1, G M Small, P B Lazarow.
Abstract
An efficient system for the import of newly synthesized proteins into highly purified rat liver peroxisomes was reconstituted in vitro. 35S-Labeled acyl-CoA oxidase (AOx) was incorporated into peroxisomes in a proteinase K-resistant fashion. This import was specific (did not occur with mitochondria) and was dependent on temperature, time, and peroxisome concentration. Under optimal conditions approximately 30% of [35S]AOx became proteinase resistant. The import of AOx into peroxisomes could be dissociated into two steps: (a) binding occurred at 0 degrees C in the absence of ATP; (b) translocation occurred only at 26 degrees C and required the hydrolysis of ATP. GTP would not substitute for ATP and translocation was not inhibited by carbonylcyanide-m-chlorophenylhydrazone, valinomycin, or other ionophores.Entities:
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Year: 1987 PMID: 3693402 PMCID: PMC2114735 DOI: 10.1083/jcb.105.6.2915
Source DB: PubMed Journal: J Cell Biol ISSN: 0021-9525 Impact factor: 10.539