scholarly journals PHYSICOCHEMICAL CHARACTERIZATION OF PITUITARY FOLLICLE-STIMULATING HORMONE

1952 ◽  
Vol 35 (4) ◽  
pp. 629-637 ◽  
Author(s):  
Choh Hao Li ◽  
Kai O. Pedersen
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Follicle Stimulating Hormone ◽  
Physicochemical Characterization ◽  
Single Protein ◽  
Pituitary Glands ◽  
The Stability ◽  
Stimulating Hormone

The physiochemical characteristics of the follicle-stimulating hormone (FSH) from whole sheep pituitary glands have been studied. The hormone behaves as a single protein in electrophoresis, diffusion, and ultracentrifugation. It has an isoelectric point at pH 4.5 and a molecular weight of 67,000 and contains 1.23 per cent hexose and 1.51 per cent hexosamine. The amino acid composition has also been determined in large part. The stability of the hormone to acid and heat has been investigated.

Isolation and characterization of β-lipolytic hormone from porcine pituitary gland

1970 ◽  
Vol 48 (9) ◽  
pp. 1017-1021 ◽  
Author(s):  
C. Gilardeau ◽  
M. Chrétien
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Pituitary Gland ◽  
Amino Acid Composition ◽  
Biological Activities ◽  
Terminal Amino Acid ◽  
Isolation And Characterization ◽  
Pituitary Glands ◽  
Terminal Amino

A lipolytic substance was isolated from porcine pituitary glands. It's amino acid composition, molecular weight, N-terminal amino acid, isoelectric point, and biological activities are reported. These results are compared to the corresponding values of sheep β-lipolytic hormone.

scholarly journals High-Sulphur Proteins From a-Keratins ll. Isolation and Partial Characterization of Purified Components From Mouse Hair

1976 ◽  
Vol 29 (2) ◽  
pp. 11 ◽  
Author(s):  
Robert C Marshall ◽  
JM Gillespie
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Fractional Precipitation ◽  
Molecular Weight Range

The present paper continues the study of the reduced and S-carboxymethylated high-sulphur proteins from mouse hair. Fractions have been obtained in a substantially purified form by fractional precipitation with ammonium sulphate at pH 6, followed by ion exchange chromatography on cellulose phosphate at pH 2�6. Approximately 80% by weight of the high-sulphur proteins fall into the ultra-high-sulphur category (carboxymethyicysteine content greater than 26 residues per 100 residues), and they cover a molecular weight range of 17000-28000. The components show a remarkable diversity in amino acid composition; for example the contents of arginine and glycine each vary by about 3 : 1. The remainder of the proteins contain 17-20 residues per 100 residues of carboxymethyicysteine, are smaller in size (molecular weight 11 500), and also show great diversity in overall amino acid composition.

DEVELOPMENT AND CHARACTERIZATION OF A HOMOLOGOUS RADIOIMMUNOASSAY FOR BOVINE FOLLICLE-STIMULATING HORMONE

1978 ◽  
Vol 77 (2) ◽  
pp. 185-193 ◽  
Author(s):  
KWONG-WAH CHENG
Keyword(s):  
Follicle Stimulating Hormone ◽  
Rabbit Antiserum ◽  
Significant Inhibition ◽  
Pituitary Glands ◽  
Stimulating Hormone

SUMMARY A radioimmunoassay for bovine FSH has been developed using a rabbit antiserum against highly purified bovine FSH (160 × NIH-FSH-S1) and a 125I-labelled tracer of the same preparation. The sensitivity was 0·25 ng/ml for purified bovine FSH or 25 ng/ml with reference to a crude bovine FSH (NIH-FSH-B1) standard. Purified bovine LH and TSH showed cross-reactivities of less than 1%, while their subunits and other purified protein hormones showed no significant inhibition at concentrations up to 100 ng/ml. Ovine FSH cross-reacted significantly but in a non-parallel manner; human and rat FSH cross-reacted only slightly. The concentrations of FSH (means ± s.e.m.) in the sera of cows (n = 12), cows at oestrus (4), bulls (7) and steers (9) were measured as 25·4 ± 4·7, 58·4 ± 12·6, 45·7 ± 9·5 and 120·2 ± 36·0 ng/ml respectively. The FSH content of bovine pituitary glands varied greatly between individuals, from 2 to 25 μg/mg tissue. The inhibition curves of pituitary and serum FSH were parallel to that of the bovine FSH standard.

scholarly journals The purification in high yield and characterization of rat hepatic glucokinase

1976 ◽  
Vol 153 (2) ◽  
pp. 363-373 ◽  
Author(s):  
M J Holroyde ◽  
M B Allen ◽  
A C Storer ◽  
A S Warsy ◽  
J M E Chesher ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Affinity Chromatography ◽  
Amino Acid Composition ◽  
Specific Activity ◽  
Sedimentation Equilibrium ◽  
High Yield ◽  
Equilibrium Studies ◽  
Enzyme Specific Activity

A new improved procedure for the purification of rat hepatic glucokinase (ATP-d-glucose 6-phosphotransferase, EC 2.7.1.2) is given. A key step is affinity chromatography on Sepharose-N-(6-aminohexanoyl)-2-amino-2-deoxy-d-glucopyranose. A homogeneous enzyme, specific activity 150 units/mg of protein, is obtained in about 40% yield. The molecular weight of the pure enzyme was determined by several procedures. In particular, sedimentation-equilibrium studies under a variety of conditions indicate a molecular weight of 48000 and no evidence for dimerization; reports in the literature of other values are discussed in the light of this evidence on the pure enzyme. The amino acid composition suggests that hepatic glucokinase is closely related to rat brain hexokinase and also the wheat “light” hexokinases.

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