Compounds > n-hydroxysuccinimidyl-5-azido-2-nitrobenzoate

n-hydroxysuccinimidyl-5-azido-2-nitrobenzoate and hydroxysuccinimidyl-4-azidobenzoate

n-hydroxysuccinimidyl-5-azido-2-nitrobenzoate has been researched along with hydroxysuccinimidyl-4-azidobenzoate* in 2 studies

Other Studies

2 other study(ies) available for n-hydroxysuccinimidyl-5-azido-2-nitrobenzoate and hydroxysuccinimidyl-4-azidobenzoate

Article	Year
Developmental change and molecular properties of somatostatin receptors in the rat cerebral cortex. Biochemical and biophysical research communications, 1989, Apr-14, Volume: 160, Issue:1 The postnatal development and molecular properties of somatostatin receptor were studied in rat cerebral cortex. With [125I-Tyr11]SRIF as a radiolabeled ligand, the specific ligand binding to crude membrane increased transiently in the early phase of postnatal development and then decreased. This increase of somatostatin binding was mainly due to the increased number of binding sites. The two subtypes classified by Tran et al., SSA and SSB, were confirmed and the studies on the relative amount of the subtypes revealed that more SSA subtype was expressed compared with SSB subtype during a week after birth, but, thereafter, both subtypes were almost equally expressed throughout the developmental stages tested. Molecular weight of the covalently labeled somatostatin receptor (SSA subtype), which was determined with the aid of the cross-linking agents, was estimated to be approximately 71,000 with no intramolecular disulfide bond. Topics: Aging; Animals; Azides; Cell Membrane; Cerebral Cortex; Cross-Linking Reagents; Female; Iodine Radioisotopes; Male; Molecular Weight; Photochemistry; Rats; Rats, Inbred Strains; Receptors, Neurotransmitter; Receptors, Somatostatin; Somatostatin; Succinimides	1989
Thyrotropin cross-links to the thyrotropin receptor through both the alpha and beta subunits. The Biochemical journal, 1986, May-01, Volume: 235, Issue:3 We have recently shown that the beta subunit of thyrotropin (TSH) can be cross-linked to the TSH receptor [Buckland, Strickland, Pierce & Rees Smith (1985) Endocrinology (Baltimore) 116, 2122-2124; Buckland, Strickland & Rees Smith (1985) Biochem. Soc. Trans. 13, 942-943]. We failed, however, to cross-link the alpha subunit to the receptor, leaving the role of this subunit in the TSH-TSH-receptor interaction uncertain. We now report the successful cross-linking of the TSH alpha subunit to the receptor by the use of two different cross-linking reagents. Our studies suggest therefore that both subunits of TSH form part of the hormone's receptor-binding site. Topics: Azides; Binding Sites; Cross-Linking Reagents; Electrophoresis, Polyacrylamide Gel; Receptors, Cell Surface; Receptors, Thyrotropin; Salicylates; Succinimides; Thyrotropin	1986

Article

Year

Developmental change and molecular properties of somatostatin receptors in the rat cerebral cortex.

Biochemical and biophysical research communications, 1989, Apr-14, Volume: 160, Issue:1

The postnatal development and molecular properties of somatostatin receptor were studied in rat cerebral cortex. With [125I-Tyr11]SRIF as a radiolabeled ligand, the specific ligand binding to crude membrane increased transiently in the early phase of postnatal development and then decreased. This increase of somatostatin binding was mainly due to the increased number of binding sites. The two subtypes classified by Tran et al., SSA and SSB, were confirmed and the studies on the relative amount of the subtypes revealed that more SSA subtype was expressed compared with SSB subtype during a week after birth, but, thereafter, both subtypes were almost equally expressed throughout the developmental stages tested. Molecular weight of the covalently labeled somatostatin receptor (SSA subtype), which was determined with the aid of the cross-linking agents, was estimated to be approximately 71,000 with no intramolecular disulfide bond.

Topics: Aging; Animals; Azides; Cell Membrane; Cerebral Cortex; Cross-Linking Reagents; Female; Iodine Radioisotopes; Male; Molecular Weight; Photochemistry; Rats; Rats, Inbred Strains; Receptors, Neurotransmitter; Receptors, Somatostatin; Somatostatin; Succinimides

1989

Thyrotropin cross-links to the thyrotropin receptor through both the alpha and beta subunits.

The Biochemical journal, 1986, May-01, Volume: 235, Issue:3

We have recently shown that the beta subunit of thyrotropin (TSH) can be cross-linked to the TSH receptor [Buckland, Strickland, Pierce & Rees Smith (1985) Endocrinology (Baltimore) 116, 2122-2124; Buckland, Strickland & Rees Smith (1985) Biochem. Soc. Trans. 13, 942-943]. We failed, however, to cross-link the alpha subunit to the receptor, leaving the role of this subunit in the TSH-TSH-receptor interaction uncertain. We now report the successful cross-linking of the TSH alpha subunit to the receptor by the use of two different cross-linking reagents. Our studies suggest therefore that both subunits of TSH form part of the hormone's receptor-binding site.

Topics: Azides; Binding Sites; Cross-Linking Reagents; Electrophoresis, Polyacrylamide Gel; Receptors, Cell Surface; Receptors, Thyrotropin; Salicylates; Succinimides; Thyrotropin

1986