Pharmacology of Isomeric Thiocyanobenzoic Acids.

Jc, Krantz; Cj, Carr; Hh, Bryant

doi:10.3181/00379727-74-17891

Cited by 4 publications

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“…The migration of rhRlx upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis was consistent with a monomeric structure, and the identity of the band was demonstrated by immunoblotting. I Iisaw's (1926) observation that a factor in the serum from pregnant guinea pigs or rabbits caused a relaxation of the pubic ligament when administered to virgin guinea pigs shortly after estrus led to the partial purification of relaxin from porcine corpora lútea (Fevold et al, 1930), but not until twenty years later was its ability to inhibit spontaneous contractions of the uterine myometrium in estrogen-primed guinea pigs (Krantz et al, 1950) and to promote cervical ripening in estrogenprimed cows (Graham & Dracy, 1953) reported.…”

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Use of recombinant DNA derived human relaxin to probe the structure of the native protein

Canova-Davis¹,

Kessler²,

Lee³

et al. 1991

Biochemistry

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This report describes the physical, chemical, and biological characterization of recombinant human relaxin (rhRlx) used as a probe to establish the disulfide pairing in native human relaxin. This strategy is necessary since native human relaxin is only available in the nanogram range. The relaxin molecule is composed of two nonidentical peptide chains, an A-chain 24 amino acids in length and a B-chain of 29 amino acids, linked by two disulfide bridges with an additional disulfide linkage in the A-chain. Native relaxin isolated from human corpora lutea was compared to rhRlx by reversed-phase chromatography, partial sequence analysis, mass spectroscopy, and bioassay. The potency of rhRlx was established by its ability to stimulate cAMP from primary human uterine endometrial cells. Native relaxin isolated from human corpora lutea was equipotent to chemically synthesized relaxin, which in turn was equipotent to rhRlx. A tryptic map was developed for rhRlx to confirm the complete amino acid sequence and assignment of the disulfide bonds. The three disulfide bonds (CysA10-CysA15, CysA11-CysB11, and CysA24-CysB23) were assigned by mass spectrometric analysis of the tryptic peptides and by comparison to chemically synthesized peptides disulfide linked in the two most probable configurations. In addition, the observed amino acid composition and sequence of rhRlx was in agreement with that predicted from the cDNA sequence with the exception that the A-chain amino terminal was pyroglutamic acid. The migration of rhRlx upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis was consistent with a monomeric structure, and the identity of the band was demonstrated by immunoblotting.

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mentioning

confidence: 99%

Use of recombinant DNA derived human relaxin to probe the structure of the native protein

Canova-Davis¹,

Kessler²,

Lee³

et al. 1991

Biochemistry

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Über die Regulierung der Schilddrüsenfunktion und die Wirkungsweise von Rhodanbenzoesäuren

Keeser

Oelschläger

1952

Archiv der Pharmazie

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Versuche jedoch, die p-Nitrophenyl-cyan-brenztraubensaureester durch Kochen mit einem UberschulJ des Alkohols bei Gegenwart der entsprechenden Natriumalkoholate umzuestern analog dem Oxalsaurediathylester verliefen negativ. J e nach der Kochzeit wurden entweder die unveranderten Ester zuriickgewonnen oder das Zersetzungsprodukt der Ester, namlich p-Nitrobenzylcyanid bzw. Benzylcyanid. Aus dem Gesagten ergeben sich somit Moglichkeiten, die Aktivitat der Schilddriise dadurch zu dampfen, daO Substanzen verabfolgt werden, die an der einen 1187

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Verfahren zur Darstellung aliphatischer, aromatischer und heterocyclischer Rhodanverbindungen aus Mercaptanen 27. Mitt.: Über organische Rhodanverbindungen

Kottke

Friedrich

Pohloudek-Fabini

1967

Archiv der Pharmazie

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Pharmacology of Isomeric Thiocyanobenzoic Acids.

Cited by 4 publications

References 0 publications

Use of recombinant DNA derived human relaxin to probe the structure of the native protein

Use of recombinant DNA derived human relaxin to probe the structure of the native protein

Über die Regulierung der Schilddrüsenfunktion und die Wirkungsweise von Rhodanbenzoesäuren

Verfahren zur Darstellung aliphatischer, aromatischer und heterocyclischer Rhodanverbindungen aus Mercaptanen 27. Mitt.: Über organische Rhodanverbindungen

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