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Plant Physiology 75:675-678 (1984)
© 1984 American Society of Plant Biologists

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Thermolysin Is a Suitable Protease for Probing the Surface of Intact Pea Chloroplasts 1

Kenneth Cline, Margaret Werner-Washburne, Jaen Andrews2 and Kenneth Keegstra

Department of Botany, University of Wisconsin, Madison, Wisconsin 53706

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 O2 evolution.

2 Present address: ARCO Plant Cell Research Institute, Dublin, CA 94566.

1 Supported in part by a grant from the United States Department of Agriculture Competitive Research Grants Office. MWW and JA were supported by National Institutes of Health grant 5 T32 GM07215.




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