tosylarginine-methyl-ester and tryptophan-methyl-ester

tosylarginine-methyl-ester has been researched along with tryptophan-methyl-ester* in 2 studies

Other Studies

2 other study(ies) available for tosylarginine-methyl-ester and tryptophan-methyl-ester

Article	Year
Inhibition of 3,5,3'-triiodothyronine binding to its receptor in rat liver by protease inhibitors and substrates. Molecular and cellular endocrinology, 1993, Volume: 93, Issue:1 Various protease inhibitors (e.g. phenylmethanesulfonyl fluoride (PMSF), tosyl-phenylalanine chloromethyl ketone (TosPheCH2Cl)) and substrates (e.g., tosyl-arginine methyl ester (TosArgOMe), tryptophan methyl ester (TrpOMe)) inhibit the binding of adrenal and sex steroids to their cognate receptors (Hubbard and Kalimi (1985) Mol. Cell. Biochem. 66, 101-109). Here we extend this finding to the receptor for 3,5,3'-triiodothyronine (T3) in rat liver nuclei. We find that PMSF, TosPheCH2Cl and other protease inhibitors as well as TosArgOMe, TrpOMe, tyrosine methyl ester (TyrOMe) and tyrosine ethyl ester (TyrOEt) inhibit binding of 125I-T3 to its receptor in rat liver nuclei. Inhibition by protease substrates appears to be at or close to the hormone binding domain. By analogy with the known mechanism of binding of protease inhibitors and substrates to enzymes, we suggest that the T3 receptor contains a nucleophilic site at or close to the hormone binding domain. Topics: Animals; Liver; Male; Molecular Structure; Phenylmethylsulfonyl Fluoride; Protease Inhibitors; Protein Binding; Rats; Rats, Wistar; Receptors, Thyroid Hormone; Structure-Activity Relationship; Sulfones; Tosylarginine Methyl Ester; Tosylphenylalanyl Chloromethyl Ketone; Triiodothyronine; Tryptophan; Tyrosine	1993
Protease substrates inhibit binding of 3H-R5020 to the G-fragment in chick oviduct cytosol. Biochemical and biophysical research communications, 1982, Oct-15, Volume: 108, Issue:3 Topics: Animals; Arginine; Cytosol; Kinetics; Molecular Weight; Norpregnadienes; Oviducts; Promegestone; Receptors, Progesterone; Time Factors; Tosylarginine Methyl Ester; Tryptophan	1982

Article

Year

Inhibition of 3,5,3'-triiodothyronine binding to its receptor in rat liver by protease inhibitors and substrates.

Molecular and cellular endocrinology, 1993, Volume: 93, Issue:1

Various protease inhibitors (e.g. phenylmethanesulfonyl fluoride (PMSF), tosyl-phenylalanine chloromethyl ketone (TosPheCH2Cl)) and substrates (e.g., tosyl-arginine methyl ester (TosArgOMe), tryptophan methyl ester (TrpOMe)) inhibit the binding of adrenal and sex steroids to their cognate receptors (Hubbard and Kalimi (1985) Mol. Cell. Biochem. 66, 101-109). Here we extend this finding to the receptor for 3,5,3'-triiodothyronine (T3) in rat liver nuclei. We find that PMSF, TosPheCH2Cl and other protease inhibitors as well as TosArgOMe, TrpOMe, tyrosine methyl ester (TyrOMe) and tyrosine ethyl ester (TyrOEt) inhibit binding of 125I-T3 to its receptor in rat liver nuclei. Inhibition by protease substrates appears to be at or close to the hormone binding domain. By analogy with the known mechanism of binding of protease inhibitors and substrates to enzymes, we suggest that the T3 receptor contains a nucleophilic site at or close to the hormone binding domain.

Topics: Animals; Liver; Male; Molecular Structure; Phenylmethylsulfonyl Fluoride; Protease Inhibitors; Protein Binding; Rats; Rats, Wistar; Receptors, Thyroid Hormone; Structure-Activity Relationship; Sulfones; Tosylarginine Methyl Ester; Tosylphenylalanyl Chloromethyl Ketone; Triiodothyronine; Tryptophan; Tyrosine

1993

Protease substrates inhibit binding of 3H-R5020 to the G-fragment in chick oviduct cytosol.

Biochemical and biophysical research communications, 1982, Oct-15, Volume: 108, Issue:3

Topics: Animals; Arginine; Cytosol; Kinetics; Molecular Weight; Norpregnadienes; Oviducts; Promegestone; Receptors, Progesterone; Time Factors; Tosylarginine Methyl Ester; Tryptophan

1982