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Partial amino acid sequence of the preprotein form of the alpha subunit of human choriogonadotropin and identification of the site of subsequent proteolytic cleavage
Authors:S Birken  J Fetherston  J Desmond  R Canfield  I Boime
Institution:1. Department of Medicine, College of Physicians & Surgeons, Columbia University, New York, N.Y. 10032 USA;1. Department of Obstetrics & Gynecology, Washington University School of Medicine, St. Louis, Missouri 63110 USA
Abstract:Messenger RNA isolated from first trimester placentae was translated using radiolabeled amino acids in both the wheat germ and the ascites cell-free systems. The choriogonadotropin α subunit product was purified by immunoprecipitation with a subunit specific antiserum. Its amino acid sequence was partially determined by automated Edman degradation analysis. An NH2-terminal extension of 24 amino acids was found and its partial sequence is:
/></figure>The preprotein form of the subunit was cleaved by the addition of microsomal membranes resulting in a homogeneous NH<sub>2</sub>-terminal product. Hence, it is unlikely that this processing step accounts for the heterogeneity that has been observed previously in the structure of this region of the subunit.</td>
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Keywords:α  alpha subunit  β  beta subunit  FSH  follitropin  hCG  choriogonadotropin  HPLC  high pressure liquid chromatography  LH  lutropin  PITC  phenylisothiocyanate  PTH  phenylthiohydantoin  RCM  reduced and carboxymethylated  SDS  sodium dodecyl sulphate
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