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Isolation of lymphocyte membrane complement receptor type two (the C3d receptor) and preparation of receptor-specific antibody.

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Formation of 11-trans slow reacting substances.

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Selective inhibition of Escherichia coli protein synthesis and growth by nonionic oligonucleotides complementary to the 3' end of 16S rRNA.

Site-specific cleavage by T1 RNase of U-1 RNA in u-1 ribonucleoprotein particles.

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Human placentas contain a specific inhibitor of RNA-directed DNA polymerase.

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Related 5S RNA transcription factors in Xenopus oocytes and somatic cells.

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Human insulin prepared by recombinant DNA techniques and native human insulin interact identically with insulin receptors.

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Human insulin prepared by recombinant DNA techniques and native human insulin interact identically with insulin receptors.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Keefer, L. M. Piron, M. A. De Meyts, P.
Abstract	Human insulin synthesized from A and B chains separately produced in Escherichia coli from cloned synthetic genes (prepared by the Eli Lilly Research Laboratories, Indianapolis, IN) was characterized by examining its interaction with human cultured lymphocytes, human circulating erythrocytes in vitro, and isolated rat fat cells. The binding behavior of the biosynthetic insulin with human cells was indistinguishable from that of native human or porcine insulins, with respect to affinity, association and dissociation kinetics, negative cooperativity, and the down-regulation of lymphocyte receptors. Similarly, the biosynthetic insulin was as potent as the native insulins in stimulating lipogenesis in isolated rat fat cells. We also examined the receptor binding characteristics of 125I-labeled human and porcine insulins monoiodinated solely at Tyr-A14, which were obtained by means of high-performance liquid chromatography of the iodination reaction mixture (this material was prepared by B. Frank, Eli Lilly Research Laboratories). In all aspects studied, the pure [TyrA14-125I]iodoinsulins were superior as tracers to the monoiodoinsulin purified by the more conventional method of gel filtration.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	3
Volume Number	78
Language	English
Publisher	National Academy of Sciences
Publisher Date	1981-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	DNA, Recombinant Metabolism Insulin Biosynthesis Receptor, Insulin Cells, Cultured Cloning, Molecular Escherichia Coli Kinetics Lymphocytes Macromolecular Substances Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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