Renal Biogenesis of Erythropoietin View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1987

AUTHORS

J. Caro , S. Schuster , A. Besarab , A. J. Erslev

ABSTRACT

The hemopoietic growth factor, erythropoietin (Epo), forms part of one of the limbs in the feed-back mechanism that control the red cell mass and adapts it to oxygen needs of the tissues (Fig. 1). The erythropoietin molecule was originally purified from urine of anemic patients by Miyake et.al. [1] and found to have a molecular weight around 38,000 daltons with a high carbohydrate content. The recent cloning of the mouse [2, 3] and human Epo [4,5] genes has indicated that the Epo molecule contained 166 amino acids with a peptide molecular weight of 18,600 daltons. There are three possible N-glycosylation sites and with the high sugar content, the total molecular weight is believed to be around 34,000 daltons. Erythropoietin is usually measured by in vitro or in vivo bioassays [6] and more recently by sensitive radioimmune assays [7,8]. More... »

PAGES

329-336

Book

TITLE

Molecular and Cellular Aspects of Erythropoietin and Erythropoiesis

ISBN

978-3-642-72654-5
978-3-642-72652-1

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-3-642-72652-1_24

DOI

http://dx.doi.org/10.1007/978-3-642-72652-1_24

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1032117974


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