Premium
Purification and properties of thiamine‐binding proteins from sesame seed
Author(s) -
Shimizu Mayumi,
Inaba Kazunari,
Yoshida Toyokazu,
Toda Takayoshi,
Iwashima Akio,
Mitsunaga Toshio
Publication year - 1995
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1034/j.1399-3054.1995.930114.x
Subject(s) - thiamine , sesamum , protein subunit , biochemistry , chemistry , arginine , amino acid , molecule , molecular mass , glutamine , disulfide bond , biology , enzyme , organic chemistry , horticulture , gene
Three thiamine‐binding proteins of 17‐19 kDa (STBP‐I, II, and III) were purified from sesame seed ( Sesamum indicum L.). Each of the proteins was composed of two subunits of equal molecular mass and each subunit consisted of a large polypeptide and a small polypeptide linked by a disulfide bond(s). They were rich in glutamic acid (or glutamine) and arginine. Their binding activities were optimal at neutral pH. They bound specifically free thiamine but not thiamine phosphates. STBP‐I had higher affinity for thiamine than STBP‐II or STBP‐III. STBP‐II and STBP‐III bound one molecule of thiamine per molecule, and STBP‐I bound 0.5 molecule. The amino acid composition and structure of the STPBs were similar to those of 2S storage proteins.