Publication | Open Access
Thermolysin Is a Suitable Protease for Probing the Surface of Intact Pea Chloroplasts
228
Citations
9
References
1984
Year
Intact Pea ChloroplastsEngineeringMolecular BiologyPlant BiochemistryPlant Molecular BiologyBiosynthesisEnvelope PolypeptidesProtein FoldingProteomicsPlant CytologyPlant BiologyBiochemistryIsolated Intact PeaPlant ProteomicsCell WallBiologySuitable ProteaseNatural SciencesBiotechnologyPotential Surface ProbesPlant Physiology
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.
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