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Biomedical subjects

C Schwabe

Publications and source records attributed to C Schwabe.

At least 73 records · Page 4Linked to original sources
PubMed1986

Relaxin on induction of parturition in beef heifers.

Purified porcine relaxin (3000 U/mg) was administered into the cervical os of primiparous beef heifers on day 278 of gestation (approximately 5 days before parturition normally occurs) to determine its effects on the induction of parturition, changes in progesterone, estrone (E1), 17 beta-estradiol (17 beta-E2), cervical dilation, and pelvic relaxation. Heifers were assigned randomly to 1 of 3 treatments: relaxin-double (two infusions of 3000 U, 12 h apart; n = 17), relaxin-single (3000 U; n = 14), and PBS-gel vehicle (n = 16). Relaxin induced marked earlier calving (P less than 0.002) than PBS-gel vehicle. The intervals between the administration of relaxin or the PBS-gel vehicle and calving were 2.0, 2.5, and 5.3 days for heifers given relaxin-double, relaxin-single, and PBS-gel vehicle, respectively. The duration of gestation was significantly reduced (P less than 0.002) in relaxin-treated heifers compared with that in control heifers. A precipitous decrease in progesterone (7.1 ng/ml) occurred in peripheral blood plasma within 24 h after relaxin treatment. Coincident with a decline in levels of progesterone, E1 and 17 beta-E2 increased by 1700 and 400 pg/ml, respectively, an increase of 35% compared with the 12% increase in these steroids in control heifers. Mean deviations of cervical dilation increased 643%, 526%, and 11% in heifers given relaxin-double, relaxin-single, and PBS-gel vehicle, respectively. Relaxin induced maximum pelvic opening between 12-36 h after treatment. Although relaxin induced significantly earlier calving, there was no incidence (0 of 31 heifers) of retained placenta. We conclude from this study that purified relaxin administered intracervically to primiparous beef heifers during late pregnancy induced premature parturition. Marked shifts of progesterone, E1, 17 beta-E2, pelvic canal expansion, and cervical relaxation reflect the premature parturition induced by relaxin.

Animals↗
PubMed1985

Naturally occurring porcine relaxins and large-scale preparation of the B29 hormone.

Porcine ovaries were collected from pregnant sows under conditions designed to keep autolysis to an absolute minimum. During the extraction the tissues were never allowed to warm up to 0 degree C until submerged in 1.6 N HCl. Isolation and fractionation of the various relaxin forms became possible by application of CM-cellulose chromatography at pH 5.5 and 7.8, gel filtration, and high-performance liquid chromatography. The new isolation procedure has made it possible to isolate and identify LeuB32 relaxin. Also, [Leu-PheA0]B29 relaxin was identified and the existence of a [Leu-PheA0]B32 relaxin may be deduced from our data. Controlled digestion of B-chain-extended relaxins with carboxypeptidase A led to the large-scale production of homogeneous B29 relaxin, a suitable starting material for controlled chemical modification of porcine relaxin.

Amino Acid Sequence↗
PubMed1985

Preparation and properties of alpha- and epsilon-amino-protected porcine relaxin derivatives.

The chemical modification of the amino groups of B29 porcine relaxin resulted in pure derivatives of N alpha A1-citraconyl-B29 relaxin, N epsilon A7, N epsilon A16, N epsilon B8-tris [[[(methylsulfonyl)ethyl]oxy]carbonyl]-B29 relaxin (Msc3-relaxin), and N alpha A1, N epsilon A7, N epsilon A16, N epsilon B8-tetrakis [[[(methylsulfonyl)ethyl]oxy]carbonyl]-B29 relaxin (Msc4-relaxin). N alpha A1-Citraconyl-B29 relaxin was obtained after selective deprotection of fully acylated B29 relaxin derivatives. The quantitative reaction of N alpha A1-citraconylrelaxin with [[(methylsulfonyl)ethyl]-oxy]carbonyl succinimide ester followed by deprotection of the citraconyl group resulted in N epsilon A7, N epsilon A16, N epsilon B8-Msc3-B29 relaxin, the starting material for selective chemical modifications at the N terminus of the relaxin A chain. In mouse interpubic ligament assay both Msc3 and Msc4 derivatives of relaxin showed a bioactivity of 30%, while in the case of N alpha A1-citraconyl-B29 relaxin the bioactivity was reduced to 15%. When compared with unmodified relaxin, only the circular dichroic spectrum of N alpha A1-citraconyl-B29 relaxin revealed significant differences. Therefore, the loss in bioactivity of the N alpha A1-citraconyl-B29 relaxin seems to be related to the structural changes caused by the introduction of a negative charge at the N terminus of the A chain.

Amino Acid Sequence↗
PubMed1985

[A0-phenylalanyl] relaxin (porcine): an active intermediate.

A [phenylalanylA0] relaxin has been isolated as a byproduct during large scale porcine relaxin preparations, using ion exchange chromatography on CM-cellulose at pH 7.8 followed by high performance liquid chromatography on reversed phase columns. The elongation at the N terminus of the A-chain has been demonstrated by amino acid and sequence analyses of the isolated and carboxymethylated relaxin-A-chain. The phenylalanyl relaxin and B29 relaxin are indistinguishable by circular dichroism spectroscopy, in mouse pubic ligament assay, and radioimmunoassay. The occurrence of phenylalanyl relaxin may be caused by an incomplete conversion of prorelaxin to relaxin.

Amino Acid Sequence↗
PubMed1984

Amino-terminal variation in melanoma antigens.

Melanoma tumors express both common antigenic determinants and individually specific markers. A melanoma-specific glycoprotein antigen ( B700 ) with a molecular weight of approximately 65,000 daltons was detected on murine B16 melanoma cells but appears on other murine and human melanoma tumors. In order to determine the relationship between the B700 antigen and other melanoma antigens which have been described and to elucidate molecular changes that have taken place in the transformation from melanocyte to melanoma, we have purified the B700 glycoprotein to homogeneity. We have carried out amino acid composition analysis and partial sequence determinations and report that the B700 melanoma antigen shows similarities to serum albumin, but is not identical to this normal component. Moreover, amino-terminal variation occurs in the first 15 residues of the B700 antigen produced by separate B16 tumors.

Amino Acid Sequence↗
PubMed1984

Cystatin. Amino acid sequence and possible secondary structure.

The amino acid sequence of cystatin, the protein from chicken egg-white that is a tight-binding inhibitor of many cysteine proteinases, is reported. Cystatin is composed of 116 amino acid residues, and the Mr is calculated to be 13 143. No striking similarity to any other known sequence has been detected. The results of computer analysis of the sequence and c.d. spectrometry indicate that the secondary structure includes relatively little alpha-helix (about 20%) and that the remainder is mainly beta-structure.

Amino Acid Sequence↗
PubMed1983

Dogfish insulin. Primary structure, conformation and biological properties of an elasmobranchial insulin.

Insulin from an elasmobranch, the spiny dogfish (Squalus acanthias) has been purified to near homogeneity by means of acid-ethanol extraction and salt precipitation. The amino acid sequences of the performic-acid-oxidised A and B chains have been determined and exhibit some unusual features. The A chain contains a total of 22 amino acids; only the insulin from coypu (a member of the Rodentia suborder, Hystricomorpha), has previously been reported to contain an extension past the A21 asparagine. The B10 histidine, which is involved in the formation of the insulin hexamers in higher vertebrates through the co-ordination of zinc, is present in this elasmobranch insulin. Several substitutions relative to bovine insulin occur in the proposed receptor binding region (A5Gln leads to His, B21Glu leads to Pro, B22Arg leads to Lys, B25Phe leads to Tyr). In spite of these substitutions, the maximal response in the rat epididymal fat cell assay is the same for bovine and dogfish insulins; the concentration required to produce the half-maximal response is, however, approximately threefold greater for dogfish insulin than that of bovine insulin. The use of interactive computer graphics model-building predicts that the dogfish insulin can attain a three-dimensional structure very similar to that of bovine insulin; circular dichroic spectra are presented which support the model-building studies.

Adipose Tissue↗
PubMed1983

N-alpha-formyl-tyrosyl-relaxin - a reliable tracer for relaxin radioimmunoassay.

Porcine relaxin has no radio-iodinatable amino acid and must therefore be modified prior to iodination. In this paper a synthesis of an iodinatable relaxin derivative is described which leads to a fairly uniform product. The nature of the modifying group (formyltyrosine) allows for easy and accurate estimation of the degree of substitution attained as well as determination of the position where substitution has occurred.

Animals↗