{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,2]],"date-time":"2025-11-02T16:06:19Z","timestamp":1762099579613},"reference-count":23,"publisher":"Wiley","issue":"1-2","license":[{"start":{"date-parts":[[2001,10,19]],"date-time":"2001-10-19T00:00:00Z","timestamp":1003449600000},"content-version":"vor","delay-in-days":4785,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["FEBS Letters"],"published-print":{"date-parts":[[1988,9,12]]},"abstract":"<jats:p>Two GTP\u2010binding proteins serving as the specific substrate of islet\u2010activating protein (IAP), pertussis toxin, were purified from human platelet membranes as heterotrimers with an \u03b1\u03b2\u03b3\u2010subunit structure. The \u03b1 of the major IAP substrate had a molecular mass of 40 kDa and differed from that of G<jats:sub>i 1<\/jats:sub> or G<jats:sub>o<\/jats:sub> previously purified from brain membranes. The partial amino acid sequences of the 40 kDa \u03b1 completely matched with the sequences which were deduced from the nucleotide sequences of the human G<jats:sub>i 2<\/jats:sub> \u03b1 gene. On the other hand, the \u03b1 of the minor IAP substrate purified from human platelets was about 41 kDa and cross\u2010reacted with an antibody raised against \u03b1 of brain G<jats:sub>i 1<\/jats:sub> (G<jats:sub>i 1<\/jats:sub> \u03b1). These results indicate that the major IAP substrate present in human platelet membranes is a product of the G<jats:sub>i 2<\/jats:sub> \u03b1 gene.<\/jats:p>","DOI":"10.1016\/0014-5793(88)80182-0","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T09:10:37Z","timestamp":1027588237000},"page":"113-117","source":"Crossref","is-referenced-by-count":29,"title":["GTP\u2010binding proteins in human platelet membranes serving as the specific substrate of islet\u2010activating protein, pertussis 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