IMMUNOCHEMICAL AND CHROMATOGRAPHIC SIMILARITY OF RAT, RABBIT, CHICKEN AND SYNTHETIC LUTEINIZING HORMONE RELEASING HORMONES

1974 ◽  
Vol 62 (1) ◽  
pp. 85-91 ◽  
Author(s):  
S. L. JEFFCOATE ◽  
P. J. SHARP ◽  
H. M. FRASER ◽  
D. T. HOLLAND ◽  
A. GUNN
Keyword(s):  
Luteinizing Hormone ◽  
Ion Exchange ◽  
Thin Layer ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Active Fraction ◽  
Luteinizing Hormone Releasing Hormone ◽  
Lh Rh ◽  
Layer Chromatography

SUMMARY Luteinizing hormone releasing hormone (LH-RH) was detected in hypothalamic extracts of rats, rabbits and chickens using a radioimmunoassay for synthetic LH-RH decapeptide. The mobilities of the immunologically active fraction and of synthetic LH-RH were the same in various chromatographic systems (gel filtration on Sephadex, thin-layer chromatography on silica gel and ion-exchange chromatography on carboxymethylcellulose) suggesting that mammalian, avian and synthetic LH-RH's are closely related.

CHROMATOGRAPHIC HETEROGENEITY OF IMMUNOREACTIVE LUTEINIZING HORMONE RELEASING HORMONE IN BLOOD FROM THE RABBIT, SHEEP AND RAT

1974 ◽  
Vol 62 (2) ◽  
pp. 333-340 ◽  
Author(s):  
S. L. JEFFCOATE ◽  
D. T. HOLLAND
Keyword(s):  
Luteinizing Hormone ◽  
Ion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Serum Samples ◽  
Blood Samples ◽  
Luteinizing Hormone Releasing Hormone ◽  
Releasing Hormone ◽  
Lh Rh

SUMMARY Serum samples from rabbits, sheep and rats containing immunoreactive luteinizing hormone releasing hormone (LH-RH) have been extracted and fractionated by ion exchange chromatography on carboxymethylcellulose followed by radioimmunoassay of the fractions. Control experiments showed that the extraction and chromatographic procedures did not alter the mobility of synthetic LH-RH. Four immunoreactive components of circulating LH-RH in blood samples from various species at various times were identified on CM-cellulose columns. One of these had a mobility identical with that of synthetic LH-RH; of the others, two were eluted before and one after synthetic LH-RH. The nature, site of formation and possible significance of the extra components are discussed.

FURTHER STUDIES ON THE NATURE OF THE IMMUNOREACTIVE LUTEINIZING HORMONE-RELEASING HORMONE (LH-RH)-LIKE PEPTIDE IN HUMAN URINE

1975 ◽  
Vol 78 (1) ◽  
pp. 232-238 ◽  
Author(s):  
S. L. Jeffcoate ◽  
Diane T. Holland
Keyword(s):  
Luteinizing Hormone ◽  
Ion Exchange ◽  
Human Urine ◽  
Chemical Nature ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Urine Samples ◽  
Luteinizing Hormone Releasing Hormone ◽  
Releasing Hormone ◽  
Lh Rh

ABSTRACT The chemical nature of the immunoreactive LH-RH-like peptide found in human urine has been investigated using ion-exchange chromatography on carboxymethyl (CM)-cellulose and a radioimmunoassay for LH-RH. A single immunoreactive substance was found in urine after LH-RH administration and in urine samples from untreated subjects. This substance did not have the mobility of either the synthetic decapeptide nor the 3–10 octapeptide on CM-cellulose and the evidence suggests that it may be the 2–10 nonapeptide of LH-RH.

Studies on an Inhibitor of Plasminogen Activation in Human Serum

1973 ◽  
Vol 30 (02) ◽  
pp. 414-424 ◽  
Author(s):  
Ulla Hedner
Keyword(s):  
Ion Exchange ◽  
Human Serum ◽  
Antithrombin Iii ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Specific Adsorption ◽  
Partial Purification ◽  
Plasminogen Activation ◽  
Preparative Electrophoresis

SummaryA procedure is described for partial purification of an inhibitor of the activation of plasminogen by urokinase and streptokinase. The method involves specific adsorption of contammants, ion-exchange chromatography on DEAE-Sephadex, gel filtration on Sephadex G-200 and preparative electrophoresis. The inhibitor fraction contained no antiplasmin, no plasminogen, no α1-antitrypsin, no antithrombin-III and was shown not to be α2 M or inter-α-inhibitor. It contained traces of prothrombin and cerulo-plasmin. An antiserum against the inhibitor fraction capable of neutralising the inhibitor in serum was raised in rabbits.

scholarly journals Chemical identity of tryptensin with angiotensin

1980 ◽  
Vol 187 (3) ◽  
pp. 647-653 ◽  
Author(s):  
K Arakawa ◽  
M Yuki ◽  
M Ikeda
Keyword(s):  
Amino Acid ◽  
Thin Layer ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Cation Exchange Chromatography ◽  
Human Plasma Protein ◽  
Plasma Protein Fraction ◽  
Layer Chromatography

Tryptensin, a vasopressor substance generated from human plasma protein fraction IV-4 by trypsin, has been isolated and the amino acid composition analysed. The procedures used for the isolation were: (a) adsorption of the formed tryptensin on Dowex 50W (X2; NH4+ form); (b) gel filtration through Sephadex G-25; (c) cation-exchange chromatography on CM-cellulose; (d) anion-exchange chromatography on DEAE-cellulose; (e) re-chromatography on CM-cellulose; (f) gel filtration on Bio-Gel P-2; (g) partition chromatography on high-pressure liquid chromatography. The homogeneity of the isolated tryptensin was confirmed by thin-layer chromatography and thin-layer electrophoresis. The amino acid analysis of the hydrolysate suggested the following proportional composition: Asp, 1; Val, 1; Ile, 1; Tyr, 1; Phe, 1; His, 1; Arg, 1; Pro, 1. This composition is identical with that of human angiotensin.

Evaluation of dialysis treatment in uremic patients by gel filtration of serum

1990 ◽  
Vol 36 (11) ◽  
pp. 1906-1910 ◽  
Author(s):  
J Osada ◽  
T Gea ◽  
C Sanz ◽  
I Millan ◽  
J Botella
Keyword(s):  
Ion Exchange ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
The Other ◽  
Control Group ◽  
Dialysis Treatment ◽  
Additional Information ◽  
Molecular Masses ◽  
Two Peaks

Abstract A group of substances of molecular masses between 300 and 1500 Da have been found to be toxic metabolites in patients with uremia. We determined the concentration in serum of these molecules in the following groups of patients: two hemodialyzed groups (one with cuprophane and the other with polyacrylonitrile dialyzers), one group treated with continuous ambulatory peritoneal dialysis, one group of nondialyzed azotemic patients, and one control group of healthy persons. Ultrafiltrates of the subjects' sera were fractionated on Sephadex G-15 followed by ion-exchange chromatography. Eluates were monitored by absorbance at 254 and 206 nm. Partially characterized peaks P1 and P2, obtained by gel filtration, correlated with the concentration of creatinine in serum; their concentrations were significantly (P less than 0.01) larger in hemodialyzed groups than in peritoneal dialyzed or in nondialyzed azotemic patients. After ion-exchange chromatography, two peaks (P'5 and P'6) correlated with serum creatinine and also were larger in hemodialyzed patients than in the other groups. Apparently, adequate discrimination is obtained by gel-filtration analysis and further analysis by ion-exchange chromatography does not provide additional information in most of the affected patients.

scholarly journals Isolation, partial purification and characterization of phospholipase A2 from Naja Katiensis venom

2021 ◽  
Vol 13 (2) ◽  
pp. 107-112
Author(s):  
C.F. Okechukwu ◽  
P.L. Shamsudeen ◽  
R.K. Bala ◽  
B.G. Kurfi ◽  
A.M. Abdulazeez
Keyword(s):  
Ion Exchange ◽  
Phospholipase A2 ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Partial Purification ◽  
Crude Venom

The most effective and acceptable therapy for snakebite victims is the immediate administration of antivenin which is limited by problems of hypersensitivity reactions in some individuals and its inability to resolve the local effects of the venom. The aim of this study was to isolate, partially purify and characterize phospholipase A2 from Naja Katiensis venom. Phospholipase A2 was partially purified via a two-step process: gel filtration on Sephadex G-75 and ion exchange chromatography using CM Sephadex, and subjected to SDS-PAGE analysis. From the results, the specific activity of the partially purified PLA2 decreased from 0.67μmol/min/mg in crude venom to 0.29μmol/min/mg after ion exchange chromatography with a yield of 5% and purification fold of 0.43. The optimum temperature of the purified PLA2 was found to be 35ºC and optimum p.H of 7. velocity studies for the determination of kinetic constants using L-a-lecithin as substrate revealed a Km  of 1.47mg/ml and Vmax  of 3.32μ moles/min/mg. The sodium dodecyl sulphate polyacrylamide gel electrophoresis of the purified PLA2 showed a distinct band with molecular weight estimated to be 14KDa. In conclusion, the present study shows that phospholipase A2 was isolated, purified and characterized. This may serve as a promising candidate for future development of a novel anti-venin drug.

THE SEPARATION AND PURIFICATION OF HUMAN LUTEINIZING AND THYROTROPHIC HORMONES

1964 ◽  
Vol 29 (1) ◽  
pp. 61-69 ◽  
Author(s):  
ANNE STOCKELL HARTREE ◽  
W. R. BUTT ◽  
K. E. KIRKHAM
Keyword(s):  
Luteinizing Hormone ◽  
Ion Exchange ◽  
Deae Cellulose ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Separation And Purification ◽  
Hormone Activity ◽  
Human Pituitary ◽  
Thyrotrophic Hormone

SUMMARY Ion-exchange chromatography was used to further purify a human pituitary fraction rich in thyrotrophic and luteinizing hormone activities. Approximately twofold concentration of both activities was obtained by chromatography on IRC-50 at pH 7·5, but the hormones were not separated. Subsequent chromatography on DEAE-cellulose at pH 9·5 led to a tenfold concentration of the luteinizing hormone in a fraction practically free of thyrotrophic activity and to a fourfold concentration of the thyrotrophic hormone in a fraction still exhibiting substantial luteinizing hormone activity.

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