The relative protein disulphide isomerase (PDI) activities of gonadotrophins, thioredoxin and PDI.
Chew
C C
CC
Department of Biochemistry, University College Galway, Ireland.
Magallon
T
T
Martinat
N
N
Lecompte
F
F
Combarnous
Y
Y
Gosling
J P
JP
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D005640:Follicle Stimulating Hormone / Q000737:chemistry / Q000378:metabolism*; D037201:Follicle Stimulating Hormone, beta Subunit; D007535:Isomerases / Q000737:chemistry / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D007986:Luteinizing Hormone / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D011489:Protein Denaturation; D019704:Protein Disulfide-Isomerases; D012260:Ribonucleases / Q000737:chemistry / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D012756:Sheep; D013552:Swine; D013879:Thioredoxins / Q000737:chemistry / Q000378:metabolism*
D037201:Follicle Stimulating Hormone, beta Subunit; D013879:Thioredoxins; D007986:Luteinizing Hormone; D005640:Follicle Stimulating Hormone; D012260:Ribonucleases; D007535:Isomerases; D019704:Protein Disulfide-Isomerases