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The Heterogeneity of the High Molecular Weight B12 Binder in Serum
- Source :
- Blood. 33:899-908
- Publication Year :
- 1969
- Publisher :
- American Society of Hematology, 1969.
-
Abstract
- The binding of vitamin B12 by serum proteins was studied by separating Co57B12-enriched serum by Sephadex gel filtration, column chromatography with DEAE-cellulose, and paper electrophoresis. Each method of separation yielded two discrete B12-binding fractions. However, the analysis of each serum by all three separation technics indicated that one of the fractions was, in each case, bipartite. The "high" molecular weight B12-binding fraction defined by Sephadex gel filtration consisted of transcobalamin I and just part of the transcobalamin II fraction. The remaining portion of transcobalamin II was eluted from Sephadex gel in a "low" molecular weight fraction. Thus, transcobalamin II, equivalent to the β-globulin B12-binder, consisted of both "high" and "low" molecular weight components. This suggests that there are at least three serum proteins that can bind vitamin B12: two β-globulins, together comprising the transcobalamin II fraction and differing in molecular weight; and transcobalamin I.
- Subjects :
- Electrophoresis
Male
Paper
Immunology
Size-exclusion chromatography
Beta-Globulins
Biochemistry
Blood serum
Column chromatography
Transcobalamin
Alpha-Globulins
Humans
Cyanocobalamin
Cellulose
Chromatography
Binding Sites
Chemistry
Blood Proteins
Cell Biology
Hematology
Blood Protein Electrophoresis
Blood proteins
Molecular Weight
Cobalt Isotopes
Vitamin B 12
Blood chemistry
Sephadex
Chromatography, Gel
Female
Subjects
Details
- ISSN :
- 15280020 and 00064971
- Volume :
- 33
- Database :
- OpenAIRE
- Journal :
- Blood
- Accession number :
- edsair.doi.dedup.....48fec5a0dd313a26bd7983b45b024778