RGD Reference Report - Rat alpha-fetoprotein heterogeneity. Comparative chemical study of the two electrophoretic variants and their Ricinus lectin-binding properties. - Rat Genome Database

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Rat alpha-fetoprotein heterogeneity. Comparative chemical study of the two electrophoretic variants and their Ricinus lectin-binding properties.

Authors: Kerckaert, JP  Bayard, B  Debray, H  Sautiere, P  Biserte, G 
Citation: Kerckaert JP, etal., Biochim Biophys Acta 1977 Aug 23;493(2):293-303.
RGD ID: 1299134
Pubmed: PMID:70227   (View Abstract at PubMed)

Two electrophoretic forms of rat alpha-fetoprotein were purified using immunosorbent chromatography and preparative electrophoresis on polyacrylamide gel slabs. Some of their respective chemical properties and their affinity for the Ricinus communis lectin (RCAI) were compared. Electrophoresis on polyacrylamide gradient gel in the presence of sodium dodecyl sulfate indicated a slight difference in molecular 74 000 for the slow alpha-fetoprotein (AFPA) and 72000 for the fat alpha-fetoprotein (AFPB). no significant difference in amino acid composition between AFPA and AFPB was found. A residue of valine was identified at the C-germinal end of both alpha-fetoproteins. The analysis of the CNRr-cleavage products reveals slight differences between AFPS and AFPB. The slow moving alpha-fetoprotein could be further fractionated on RCAI-sepharose column in two components, AFPA1 and AFPA2 differing by their sialic acid content.

Objects referenced in this article
Gene Myc MYC proto-oncogene, bHLH transcription factor Rattus norvegicus
Gene Pdx1 pancreatic and duodenal homeobox 1 Rattus norvegicus

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