STUDIES ON THE NATURE OF MAMMALIAN HYPOTHALAMIC THYROTROPHIN RELEASING HORMONE USING IMMUNOCHEMICAL, CHROMATOGRAPHIC AND ENZYMIC TECHNIQUES

1975 ◽  
Vol 65 (1) ◽  
pp. 83-90 ◽  
Author(s):  
S. L. JEFFCOATE ◽  
N. WHITE
Keyword(s):  
Ion Exchange ◽  
Human Plasma ◽  
Carboxymethyl Cellulose ◽  
Mammalian Species ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Normal Human Plasma ◽  
Thyrotrophin Releasing Hormone ◽  
Releasing Hormone ◽  
Normal Human

SUMMARY Hypothalamic extracts from three mammalian species (rat, rabbit and sheep) were found to contain several ng of immunoreactive thyrotrophin releasing hormone (TRH)-like activity. This substance chromatographed on ion exchange chromatography (carboxymethyl cellulose) as a single peak that was indistinguishable from synthetic TRH. Hypothalamic TRH was also inactivated by normal human plasma at a rate (1·21–1·46%/μl plasma/h and 1·59–1·77%/50 μl plasma/min) similar to that of synthetic TRH (1·42%/μl plasma/h and 1·73%/50 μl plasma/min). This combination of chromatographic and enzymic techniques can be applied to the identification of immunoreactive TRH in body fluids.

Studies on γA-globulins and α2-macroglobulins. Characterization of γA- and α2-macroglobulins

1968 ◽  
Vol 46 (3) ◽  
pp. 211-216 ◽  
Author(s):  
Benjamin E. Sanders ◽  
Yang H. Oh
Keyword(s):  
Ion Exchange ◽  
Physicochemical Properties ◽  
Human Plasma ◽  
Molecular Sieve ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Normal Human Plasma ◽  
Γ Globulins ◽  
Normal Human

Fractionation into several individual components was achieved from Cohn's Fraction III of human plasma by the successive application of separation principles that depend on solubility, charge, and size (precipitation, ion-exchange chromatography, and molecular-sieve chromatography methods). Characterization was made by various electrophoretic procedures such as microzone on cellulose acetate, disc on acrylamide gel, and immunoelectrophoresis, and includes some physicochemical properties of the purified proteins. There are found to be various components of γ-globulins, α2-macroglobulins, β-glycoproteins, β-lipoproteins, and other minor proteins in Cohn's Fraction III of normal human plasma. The physicochemical properties of two γA-globulins and two α2-macroglobulins were investigated.

Isolation of 2-Acetamido-1-β-(L-β-Aspartamido)-1,2-Dideoxy-D-Glucose from Normal Human Urine

1972 ◽  
Vol 18 (9) ◽  
pp. 951-955 ◽  
Author(s):  
Barbara O’Neill Rowley ◽  
Paul B Hamilton
Keyword(s):  
Ion Exchange ◽  
Human Urine ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Normal Individuals ◽  
Normal Human ◽  
Elution Behavior ◽  
Solvent Systems ◽  
And Migration ◽  
Layer Chromatography

Abstract A glycopeptide was isolated from normal human urine by fractionation on a column of Sephadex G-10 and preparative ion-exchange chromatography. Elution behavior during ion-exchange chromatography in two different solvent systems, amino acids formed upon hydrolysis, and migration on high-voltage electrophoresis and thin-layer chromatography were essentially identical for this substance and for authentic 2-acetamido-l-β-(L-β-aspartamido)-1,2-dideoxy-D-glucose. A technique was developed to permit analytical-scale fractionation of individual urines followed by analysis for this glycopeptide; urine from two normal individuals contained 7 and 11 µmol of 2-acetamido-1-β-(L-β-aspartamido)-1,2-dideoxy-D-glucose per liter.

scholarly journals Isolation of albumin from whole human plasma and fractionation of albumin-depleted plasma

1976 ◽  
Vol 157 (2) ◽  
pp. 301-306 ◽  
Author(s):  
J Travis ◽  
J Bowen ◽  
D Tewksbury ◽  
D Johnson ◽  
R Pannell
Keyword(s):  
Ion Exchange ◽  
Human Plasma ◽  
Plasma Proteins ◽  
Deae Cellulose ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Affinity Column ◽  
Plasma Albumin ◽  
Cibacron Blue ◽  
Blue Sepharose

The dye Cibacron Blue F-3-GA was conjugated to Sepharose to provide an affinity column for serum albumin. Passage of whole human plasma through a column of Cibacron Blue-Sepharose results in the removal of approx. 98% of the albumin. The latter can be quantitatively recovered by desorption with NaSCN. Albumin-depleted plasma can be readily resolved into discrete fractions by a combination of conventional biochemical techniques. In particular, the resolution of plasma proteins with properties similar to those of native human plasma albumin can readily be accomplished by ion-exchange chromatography of the Sepharose-dye-treated plasma on DEAE-cellulose.

Direct recovery of clotting factor IX from unclarified human plasma by expanded bed ion exchange chromatography

2006 ◽  
Vol 30 (2) ◽  
pp. 138-146 ◽  
Author(s):  
Yu-Kaung Chang ◽  
Jim-Tong Horng ◽  
Ren-Ze Huang ◽  
Shiuan-Yaw Lin
Keyword(s):  
Ion Exchange ◽  
Human Plasma ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Factor Ix ◽  
Clotting Factor ◽  
Expanded Bed

scholarly journals Oxidation-labile subfraction of human plasma low density lipoprotein isolated by ion-exchange chromatography

1991 ◽  
Vol 32 (5) ◽  
pp. 763-774
Author(s):  
H Shimano ◽  
N Yamada ◽  
S Ishibashi ◽  
H Mokuno ◽  
N Mori ◽  
...  
Keyword(s):  
Ion Exchange ◽  
Human Plasma ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Low Density

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.

THE PURIFICATION OF TRYPSINOGEN BY ION-EXCHANGE CHROMATOGRAPHY

1962 ◽  
Vol 40 (5) ◽  
pp. 555-564
Author(s):  
L. B. Smillie ◽  
G. Y. Mabbott ◽  
G. R. Neufeld
Keyword(s):  
Ion Exchange ◽  
Trypsin Inhibitor ◽  
Carboxymethyl Cellulose ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Soybean Trypsin Inhibitor ◽  
Physical Parameters ◽  
Tryptic Activity ◽  
Potential Activity ◽  
Chymotryptic Activity

The purification of trypsinogen by several methods of ion-exchange chromatography has been investigated. The use of phosphate–urea buffers on Bio-Rex 70 was not a suitable preparative procedure because of considerable inactivation of the zymogen. Chromatography on carboxymethyl cellulose at pH 3.2 produced no significant increase in the potential tryptic activity. In the presence of soybean trypsin inhibitor, trypsinogen was successfully chromatographed on Bio-Rex 70 to yield a product of high potential activity and of low free tryptic and chymotryptic activity. It was essentially free from soybean trypsin inhibitor and possessed the physical parameters previously published for this protein.

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