Detail of "33289-76-8"

Reference

Characterization of soluble bradykinin receptor-like binding sites

Characterization of soluble bradykinin receptor-like binding sites. Fredrick, Mark J.; Odya, Charles E. (Pharmacol. Sect., Indiana Univ., Bloomington, IN 47405, USA). Eur. J. Pharmacol., 134(1), 45-52 (English) 1987. CODEN: EJPHAZ. ISSN: 0014-2999. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) Bradykinin (BK) [58-82-2] receptor-like binding sites were solubilized from a particulate fraction of bovine uterine myometrium (BUM) using the zwitterionic detergent CHAPS. Scatchard anal. of 125I-labeled [Tyr1]kallidin (T1K) [33289-76-8] binding revealed a single class of sol. binding sites with equil. dissocn. const. = 0.35 nM and max. binding capacity = 0.13 pmol/mg protein. The sol. binding sites exhibited a kinin-binding specificity comparable to that of the particulate BUM receptor-like sites. Sol. T1K binding assocn. kinetics were 1st-order at the 4 T1K concns. examd. A plot of the pseudo-1st order rate const. vs. T1K concn. was linear, and values for the assocn. and dissocn. (k-1) rate consts. were obtained. These rate consts. yielded a kinetically derived equil. dissocn. const. (0.64 nM) which was comparable to that obtained by Scatchard anal. Biphasic dissocn. of bound T1K was resolved into rapid and slow dissocn. phases. 32222-00-7 and 550-19-6 which are cas registry numbers of substances are two of reagents here. The rate const. (k-1) of the rapid dissocn. phase was comparable to the dissocn. rate const. detd. in assocn. expts. A biphasic loss of sol. T1K binding activity was obsd. with storage at 10°. .

Interactions of kinins with angiotensin I converting enzyme (kininase II)

Interactions of kinins with angiotensin I converting enzyme (kininase II). Odya, Charles E.; Wilgis, Ford P.; Vavrek, Ray J.Several substances are used for example 9015-82-1 and 51770-53-7 which are their cas registry numbers.; Stewart, John M. (Sch. Med., Indiana Univ., Bloomington, IN 47405, USA). Biochem. Pharmacol., 32(24), 3839-47 (English) 1983. CODEN: BCPCA6. ISSN: 0006-2952. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) Angiotensin I converting enzyme (ACE) [9015-82-1] was purified to homogeneity from porcine kidney to det. whether iodobradykinins bind to the enzyme and, if so, whether SQ20881 [35115-60-7], a competitive ACE inhibitor, changes the conformation of the enzyme in such a way that it binds kinins with an affinity and specificity expected of a bradykinin (BK) receptor, i.e. where the BK-potentiating action of SW20881 involves an increase in the no. of BK receptors due to a conformational change in ACE. 125I-labeled derivs. of 1-tyrosine-kallidin (TIK) [33289-76-8] and 8-tyrosine-BK [32222-00-7] bound to the EDTA-inhibited enzyme, and binding was inhibited by nonradioactive BK. 125I-labeled 5-tyrosine-BK was not bound by the enzyme. Specificity of TIK binding was tested with 48 BK analogs, and the concns. of analogs that inhibited 50% of TIK binding were detd. BK at 1.6 ′ 10-8 M inhibited 50% of TIK binding. In addn., the concns. of analogs that decreased by 50% the rate of 3H-labeled Hip-Gly-Gly ([3H]-HGG) [31384-90-4] hydrolysis by ACE were assessed. BK at 1.2 ′ 10-6 M decreased the rate of [3H]-HGG hydrolysis by 50%. A comparison between these concns. of analogs for inhibition of TIK binding and [3H]-HGG hydrolysis yielded a high correlation coeff. The specificity of ACE binding was clearly different from that expected of a BK receptor. Compds. structurally unrelated to BK, such as SQ20881, pGlu-Lys-Trp-Ala-Pro-OH [30505-63-6], and angiotensin I [484-42-4], inhibited TIK binding and [3H]-HGG hydrolysis by ACE. .