The isolation and purification of an ovarian polypeptide with uterin-relaxing activity

Griss, G.; Keck, James L.; Engelhorn, R.; Tuppy, H.

doi:10.1016/0005-2795(67)90380-7

Cited by 35 publications

(11 citation statements)

References 18 publications

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“…Rabbit placentas, obtained from Pel-Freeze, Inc. (Roger, AR), were extracted using the procedure of Griss et al [14]. Partially frozen placentas were homogenized with a Polytron (model no.…”

Section: Tissue Extractionmentioning

confidence: 99%

B-Chain Sequence and In Situ Hybridization of the Rabbit Placental Relaxin-Like Gene Product

Fields

Lee²,

Jetten³

et al. 1999

Biology of Reproduction

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We reported that the nucleotide sequence of a cDNA generated from rabbit placental poly(A)(+) RNA using porcine preprorelaxin primers was identical to SQ10, a product of squamous differentiated tracheal epithelial cells. However, these results did not confirm that SQ10 was the biologically active rabbit relaxin that had been isolated previously yet not sequenced. In this study, a 7-kDa protein isolated from rabbit placentas exhibited relaxin bioactivity and cross-reacted with a porcine relaxin antiserum. A partial amino acid sequence of this protein revealed a sequence identical to that of SQ10. Although the amino acid sequence of the putative relaxin receptor-binding domain found in the B chain of relaxin was modified in SQ10 from CGRDYVR to CRNDFVR, the placental protein was bioactive. These results suggest that SQ10 is the rabbit relaxin. In situ hybridization, using an SQ10 riboprobe, indicated radiolabeling in the syncytiotrophoblast cells of the rabbit placenta. The pattern of labeling corresponded with the immunohistochemical staining for relaxin observed with use of a porcine relaxin antiserum. These results indicate that the syncytiotrophoblast cells are a site of synthesis for SQ10 and that the immunostaining is not solely the result of sequestering SQ10 through receptor-mediated endocytosis. A potential role for relaxin in implantation is discussed.

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Section: Tissue Extractionmentioning

confidence: 99%

B-Chain Sequence and In Situ Hybridization of the Rabbit Placental Relaxin-Like Gene Product

Fields

Lee²,

Jetten³

et al. 1999

Biology of Reproduction

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“…Since its discovery by Hisaw (1926), relaxin has been considered to be a hormone which was primarily associated with pregnancy (Hall, 1960;Belt, Anderson, Cavazos & Melampy, 1971), and the ovary of the pregnant sow has been considered as a rich source of relaxin (Fevold, Hisaw & Meyer, 1930;Griss, Keck, Engelhorn & Tuppy, 1967;Belt et al, 1971). Many investigators considered that this hormone was solely a product of the corpus luteum (Belt et al, 1971;Anderson, Ford, Melampy & Cox, 1973), but isolation studies of pregnant sow ovaries have indicated that relaxin can exhibit microheterogeneity (Sherwood & O'Byrne, 1974).…”

Section: Introductionmentioning

confidence: 99%

Identification of relaxins in porcine follicular fluid and in the ovary of the immature sow

Matsumoto¹,

Chamley²

1980

Reproduction

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“…Separation was on a sorbitol gradient using pH 7-9 and 9-11 carrier ampholytes. (4) 0.014 ± 0.003 (2) 0.017 ± 0.004 (2) 0.013 ± 0.003 (2) Four batches of CL from 129 ovaries with a total weight of 545 g were extracted (12).…”

Section: Resultsmentioning

confidence: 99%

“…Three 15-sec bursts at full speed were used to completely disrupt the tissue. Five additional volumes of the extraction solution was added, and the slurry was incubated at 4 C for 24 h. Insoluble tissues were removed by centrifugation at 39,000 X g for 20 min at 4 C. The original procedure (12) used 300 rpm. This increased speed aided in the removal of a large proportion of insoluble material which would reduce the specific activity of the hormone in the final extract.…”

mentioning

confidence: 99%

Evidence For Relaxin in Corpora Lutea of Late Pregnant Cows*

Fields

Castro-Hernandez

et al. 1980

Endocrinology

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Relaxin was isolated from corpora lutea of third trimester pregnant cows. Fractions having relaxin activity eluted in the 6000 and 1400 molecular weight ranges when chromatographed on Bio-Gel P-10. Both fractions were shown to inhibit spontaneous contractions of the mouse uterus, and the 6000 molecular weight fraction promoted formation of the mouse interpubic ligament. Agar diffusion studies with an antiserum to purified porcine relaxin showed a continuous precipitin line with no spurring between the two bovine relaxin fractions and NIHR-P1 porcine relaxin standard. Electrofocusing of the 6000 molecular weight fraction demonstrated three fractions which were capable of inhibiting contractions of the mouse uterus and which cross-reacted with porcine relaxin antiserum. The isoelectric points of these three fractions were 8.8, 10.1, and 11.5. Large luteal cells in corpora lutea from cows in the midtrimester of pregnancy were detected that gave a positive stain for relaxin with the immunoperoxidase method.

show abstract

The isolation and purification of an ovarian polypeptide with uterin-relaxing activity

Cited by 35 publications

References 18 publications

B-Chain Sequence and In Situ Hybridization of the Rabbit Placental Relaxin-Like Gene Product

B-Chain Sequence and In Situ Hybridization of the Rabbit Placental Relaxin-Like Gene Product

Identification of relaxins in porcine follicular fluid and in the ovary of the immature sow

Evidence For Relaxin in Corpora Lutea of Late Pregnant Cows*

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