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

Kenneth Cline | Zendy; Margaret WernerWashburne | Zendy; Jaen Andrews | Zendy; Kenneth Keegstra | Zendy

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

Author(s) -

Kenneth Cline,

Margaret WernerWashburne,

Jaen Andrews,

Kenneth Keegstra

Publication year - 1984

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.75.3.675

Subject(s) - thermolysin , pisum , proteases , pronase , chloroplast , biochemistry , biology , protease , chymotrypsin , sativum , trypsin , chemistry , botany , enzyme , gene

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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