Separation of cobalamin analogues in human sera binding to intrinsic factor and to R-type vitamin B12 binders.

Abstract:

:Intrinsic factor (IF) and cobalamin-R-binding protein (R-binder) linked to polyacrylamide beads were used to absorb cobalamins from solutions and serum extracts. Both binding agents were equally effective in removing [57Co]B12 from aqueous solution. IF was more effective than R-binder in removing [57Co]B12 added to a serum extract. All endogenous cobalamins detectable in serum by saturation analysis assay were removed by absorption onto R-binder. Absorption with IF removed microbiologically-active cobalamins but left behind analogues assayable with an R-binder. However, when absorption with IF was continued the concentration of R-binding cobalamins steadily declined indicating that IF bound both types of cobalamins through the binding was less avid for the microbiologically-inactive analogues than for microbiologically-active cobalamins. Finally, the R-binding analogues in serum were carried on transcobalamin I and none was detectable on transcobalamin II. The absorption studies establish the presence of two types of cobalamins one binding preferentially to IF and the other preferentially to R-binder. Only the former is detected by microbiological assay.

journal_name

Br J Haematol

authors

Muir M,Chanarin I

doi

10.1111/j.1365-2141.1983.tb02141.x

subject

Has Abstract

pub_date

1983-08-01 00:00:00

pages

613-21

issue

4

eissn

0007-1048

issn

1365-2141

journal_volume

54

pub_type

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