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November 1, 1986Journal of Biological ChemistryOpen Access

The lipid binding, regulatory domain of protein kinase C. A 32-kDa fragment contains the calcium- and phosphatidylserine-dependent phorbol diester binding activity.

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Abstract

Trypsinization of rat brain protein kinase C (80 kDa) into 50-and 32-kDa fragments occurred

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Cite This Study

Lee et al. (1986) studied this question.

synapsesocial.com/papers/6a23c2d09e1c90a91c09345a https://doi.org/10.1016/s0021-9258(18)66795-x

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Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

1Phorbol ester binding and activation of protein kinase C on triton X-100 mixed micelles containing phosphatidylserine.Original Research · 1986 · 127 citations
2Receptor-mediated Modulation of Human Monocyte, Neutrophil, Lymphocyte, and Platelet Function by Phorbol DiestersIn Vitro Study · 1982 · 77 citations
3Evidence that treatment of platelets with phorbol ester causes proteolytic activation of Ca2+‐activated, phospholipid‐dependent protein kinaseOriginal Research · 1985 · 120 citations
4Activation of protein kinase C by Triton X-100 mixed micelles containing diacylglycerol and phosphatidylserine.Original Research · 1985 · 469 citations