Charge forms of Wistar rat alpha-lactalbumin. A contradiction

alpha-Lactalbumin was purified from the milk of Wistar rats and was compared to that obtained from Fisher 344 rats. alpha-Lactalbumin isolated from the Wistar rat exists as two forms which differ in their sialic acid content, as the desialyated forms migrate to one identical position on polyacrylami...

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Bibliographic Details
Published in:The Journal of biological chemistry 1980-06, Vol.255 (12), p.5834-5837
Main Authors: Prasad, R, Ebner, K E
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino Acids - analysis
Animals
Electrophoresis, Polyacrylamide Gel
Female
Lactalbumin - isolation & purification
Molecular Weight
Pregnancy
Rats
Sialic Acids - analysis
Species Specificity
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Summary:alpha-Lactalbumin was purified from the milk of Wistar rats and was compared to that obtained from Fisher 344 rats. alpha-Lactalbumin isolated from the Wistar rat exists as two forms which differ in their sialic acid content, as the desialyated forms migrate to one identical position on polyacrylamide gels. These two charge forms are identical with the charge Forms II and III previously characterized from Fisher rat alpha-lactalbumin. No evidence was found to verify previous reports that one form of the Wistar rat alpha-lactalbumin had a higher molecular weight than the other form. Indeed, the molecular weights and the amino acid compositions of the two forms of Wistar rat alpha-lactalbumin are identical. In addition, the partial amino acid sequence at the NH2-terminal end and the amino acid composition of the COOH-terminal cyanogen bromide peptide of the two forms are identical. The results in this study contradict those reported previously and show that rat alpha-lactalbumin exists as a single molecular weight species.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)70704-2