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Science 23 December 1988:
Vol. 242. no. 4886, pp. 1697 - 1700
DOI: 10.1126/science.3201259
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Articles

Science, Vol 242, Issue 4886, 1697-1700
Copyright © 1988 by American Association for the Advancement of Science

articles

Molecular cloning of two types of GAP complementary DNA from human placenta

M Trahey, G Wong, R Halenbeck, B Rubinfeld, GA Martin, M Ladner, CM Long, WJ Crosier, K Watt, K Koths, and al. et

Department of Molecular Biology, Cetus Corp., Emeryville, CA 94608.

The ras p21 GTPase-activating protein (GAP) was purified from human placental tissue. Internal amino acid sequence was obtained from this 120,000-dalton protein and, by means of this sequence, two types of complementary DNA clones were isolated and characterized. One type encoded GAP with a predicted molecular mass of 116,000 daltons and 96% identity with bovine GAP. The messenger RNA of this GAP was detected in human lung, brain, liver, leukocytes, and placenta. The second type appeared to be generated by a differential splicing mechanism and encoded a novel form of GAP with a predicted molecular mass of 100,400 daltons. This protein lacks the hydrophobic amino terminus characteristic of the larger species, but retains GAP activity. The messenger RNA of this type was abundantly expressed in placenta and in several human cell lines, but not in adult tissues.


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Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteins.
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A Kazlauskas, C Ellis, T Pawson, and J. Cooper (1990)
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Recombinant 47-kilodalton cytosol factor restores NADPH oxidase in chronic granulomatous disease.
K. Lomax, T. Leto, H Nunoi, J. Gallin, and H. Malech (1989)
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Regulatory Proteins of R-Ras, TC21/R-Ras2, and M-Ras/R-Ras3.
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