Thyroid hormone binding protein contains glycosylation site binding protein activity.
Several lines of evidence provided by other workers indicate that within the same species thyroid hormone binding protein, the beta-subunit of prolyl hydroxylase, and protein disulfide isomerase are the same protein. We sought to determine if glycosylation site binding protein, a lumenal protein of the endoplasmic reticulum, also has the same primary structure. To accomplish this the level of glycosylation site binding protein (GSBP) activity, measured by photolabeling with a glycosylation site peptide probe, was carried out in preparations of 3T3 cells and in E. coli transformed with human thyroid hormone binding protein cDNA. The results strongly support the idea that GSBP is identical to these other lumenal proteins of the endoplasmic reticulum.
Department of Biochemistry and Cell Biology, SUNY at Stony Brook, NY 11794-5215.
H
H
Kimura
R
R
Noiva
T
T
Mizunaga
K
K
Yamauchi
R
R
Horiuchi
S Y
SY
Cheng
W J
WJ
Lennarz
D000345:Affinity Labels; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D002460:Cell Line; D004926:Escherichia coli / Q000235:genetics; D005456:Fluorescent Dyes; D006031:Glycosylation; D006801:Humans; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D013963:Thyroid Hormones; D014170:Transformation, Genetic; D014284:Triiodothyronine / Q000378:metabolism*; D000097810:Thyroid Hormone-Binding Proteins
D000345:Affinity Labels; D002352:Carrier Proteins; D005456:Fluorescent Dyes; D008565:Membrane Proteins; D013963:Thyroid Hormones; D014284:Triiodothyronine; D000097810:Thyroid Hormone-Binding Proteins