Detail of "12279-41-3"

Reference

Cortisol production by dispersed guinea-pig adrenal cells; a specific, sensitive and reproducible response to ACTH and its fragments

Cortisol production by dispersed guinea-pig adrenal cells; a specific, sensitive and reproducible response to ACTH and its fragments. Lambert, A.; Frost, J.; Garner, C.; Robertson, W. R. (Hope Hosp., Univ. Manchester, Salford M6 8HD, UK). J. Steroid Biochem., 21(2), 157-62 (English) 1984. CODEN: JSTBBK. ISSN: 0022-4731. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) Naturally occurring steroids and peptide hormones, tested at supraphysiol. concns., were without effect on basal and human 1-39 ACTH (h 1-39) [12279-41-3] (25 ng/L)-stimulated cortisol [50-23-7] prodn. Further, low concns. of angiotensinII [11128-99-7], pro-opiocortin [66796-54-1] N-terminal fragment 1-76 and g-MSH [72711-43-4], all of which were reported to synergize with ACTH with regard to cortisol prodn., were without effect alone or in combination with ACTH over the range 2.2 ′ 10-13-5.5 ′ 10-12M. The activity of h 1-39 was compared with that of the ACTH related peptides 1-24 [16960-16-0], 1-18 [1285-85-4], 1-17 [7266-47-9], 1-16 [5576-42-1], 1-13-NH2 (a MSH) [37213-49-3], 1-10 [2791-05-1], and 4-10 [4037-01-8]. The dose responses were parallel and the same maximal cortisol output was obsd. with all the peptides except the 1-10 fragment. Half maximal stimulation occurred at 3.1 ′ 10-12 (1-24), 4.4 ′ 10-12 (h 1-39), 1.5 ′ 10-11 (1-39), 3.3 ′ 10-10 (1-18), 5 ′ 10-9 (1-13-NH2), 8 ′ 10-9 (1-17), 2 ′ 10-7 (1-16), and 1 ′ 10-5 (4-10) M resp. Interference by the above ACTH-derived peptides in cortisol secretion by the cells in response to 5.5 ′ 10-12M h 1-39 was minimal over the range 5.2 ′ 10-12-2.2 ′ 10-6M. The sensitivity of the adrenal cells to h 1-39 was such that 2 ng/L provoked cortisol secretion over the control. The relative std. deviation within assay for each dose on the full std. curve (2.2 ′ 10-13-1.1 ′ 10-10M) was <10%. Half maximal stimulation was given by 14.5 ng/L. Between control and 1.1 ′ 10-10M ACTH there was a 32-fold change in cortisol prodn.

Adrenocorticotropin radioimmunoassay: properties of antisera against synthetic ACTH(1-24) and its clinical application

Adrenocorticotropin radioimmunoassay: properties of antisera against synthetic ACTH(1-24) and its clinical application. Khan, M. N.; Mirel, R. D.; Ontjes, D. A.; Ghosh, A. P.; Lazarus, L. H.; DiAugustine, R. P. (Lab. Pulmon. Funct. Toxicol., Natl. Inst. Environ. Health Sci., Research Triangle Park, NC, USA). Horm. Res., 20(2), 129-37 (English) 1984. CODEN: HRMRA3. ISSN: 0301-0163. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) Two antiserums against synthetic ACTH(1-24) [16960-16-0] developed in rabbits showed strikingly different affinities toward the ACTH mol. Both antiserums (A-6 and A-7) were highly specific for the COOH-terminal region of ACTH(1-24). Antiserum A-6 recognized human ACTH(1-39) [12279-41-3] poorly. RIAs using these antiserums permitted the rapid (￡18 h) quantitation of ACTH(1-24) (A-6) or ACTH(1-39) (A-7) at picogram levels. ACTH levels were detd. on silicic acid exts. of rat and human plasma samples by the RIA specific for the mid-region of ACTH(1-39) (A-7) and compared with that obtained by an ACTH(34-39) (C-terminal) RIA. In nearly all cases the C-terminal/mid-region ACTH ratios were <1.0, indicating that C-terminus of ACTH is more readily degraded by tissue or blood peptidases than are internal sequences. A solid-phase immunoadsorbent RIA specific for the extreme COOH-terminus of ACTH(1-24) was developed by coupling antiserum (A-6) to Sepharose 4B. This assay exhibited the same specificity as the sol. antiserum, yet tolerated relatively high concns. of protein. Although the assay was suitable for rapid quantitation of ACTH(1-24), a decrease in sensitivity was obsd. in comparison to a conventional assay.