Isolation and characterization of thiamin-binding protein from chicken egg white

Abstract

A thiamin-binding protein was isolated and characterized from chicken egg white by affinity chromatography on thiamin pyrophosphate coupled to aminoethyl-Sepharose. The high specificity of interaction between the thiamin-binding protein and the riboflavin-binding protein of the egg white, with a protein/protein molar ratio of 1.0, led to the development of an alternative procedure that used the riboflavin-binding protein immobilized on CNBr-activated Sepharose as the affinity matrix. The thiamin-binding protein thus isolated was homogeneous by the criteria of polyacrylamide-gel disc electrophoresis, double immunodiffusion and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, had a mol.wt. of 38,000 +/- 2000 and was not a glycoprotein. The protein bound [14C]thiamin was a molar ratio of 1.0, with dissociation constant (Kd) 0.3 micrometer.

Purification and some properties of thiamine-binding protein from rice bran.

“…The exact function of these thiamine binding proteins in microorganisms is still unknown, however, evidence for their involvement in thiamine transport has been discussed (7). Recently , some thiamine binding proteins have been found in animal tissues such as chicken egg white (8) and liver (9), and it has been supposed that the binding protein in chicken egg white has a role in the deposition and transport of thiamine for the proper growth and development of chick embryo. On the other hand, a previous communication from this laboratory has indicated that there exists a thiamine-binding protein in rice bran, which was the first observation made on a plant (10) (Osaka).…”

Properties of thiamin‐binding proteins from sesame seed 2S albumins

“…Thiamin‐binding proteins (TBPs) found in plant seeds bind only free thiamin and are assumed to be seed storage proteins because of their localization in plant seeds (Nishimura et al 1984a), although the TBPs from microorganisms and animal tissues bind both free thiamin and thiamin phosphates and are involved in thiamin transport (Iwashima et al 1979; Muniyamppa and Adiga 1979). Sesame seeds have two 17‐kDa TBPs, termed STBP‐I and ‐II, and a 19‐kDa TBP, termed STBP‐III (Shimizu et al 1995).…”

Isolation and characterization of riboflavin-binding protein from pregnant-rat serum

“…They were exposed to a 14h-0h light-dark schedule. The sources of other biochemicals and reagents were detailed elsewhere (Muniyappa & Adiga, 1979).…”