| Literature DB >> 16663686 |
K Cline1, M Werner-Washburne, J Andrews, K Keegstra.
Abstract
Several proteases, i.e., pronase, a mixture of trypsin and chymotrypsin, and thermolysin were screened as potential surface probes of isolated intact pea (Pisum sativum var Laxton's Progress No. 9) chloroplasts. Of these, only thermolysin met the criteria of a suitable probe. Thermolysin destroyed outer envelope polypeptides, but did not affect inner envelope polypeptides, envelope permeability properties or such chloroplast activities as metabolite transport and O(2) evolution.Entities:
Year: 1984 PMID: 16663686 PMCID: PMC1066975 DOI: 10.1104/pp.75.3.675
Source DB: PubMed Journal: Plant Physiol ISSN: 0032-0889 Impact factor: 8.340