ISSN:
1573-4927
Keywords:
Bovine
;
transferrin
;
phentotypes
;
fragments
;
electrophoresis
;
neuraminidase
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Abstract Iron-saturated bovine transferrins A, D1, D2, and E were cleaved by trypsin yielding monoferric fragments. The N-terminal fragments (F) of transferrins A and D2 had identical mobility in cellulose acetate electrophoresis, that of transferrin D1 a slower mobility, and that of E a still slower mobility. The C-terminal fragments (S) gave multiple bands which were essentially identical in the case of transferrins A, D1, and E, but of slower mobility in the case of transferrin D2. All four variants had identical N-terminal amino acid sequences. The electrophoretic mobility of the C-terminal fragments was reduced by neuraminidase treatment, but the N-terminal fragments were unaffected. The four transferrin variants therefore appear to be made up from three electrophoretically distinguishable N-terminal halves and two C-terminal halves. The feature responsible for the electrophoretic double banding of homozygous bovine asialotransferrins is consistently associated with the C-terminal half of the molecule.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00500118
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