Purification and characterization of follicle-stimulating hormone from pituitary glands of sea bass (Dicentrarchus labrax)

2008 ◽  
Vol 158 (1) ◽  
pp. 68-76 ◽  
Author(s):  
Gregorio Molés ◽  
Ana Gómez ◽  
Ana Rocha ◽  
Manuel Carrillo ◽  
Silvia Zanuy
Keyword(s):  
Follicle Stimulating Hormone ◽  
Dicentrarchus Labrax ◽  
Sea Bass ◽  
Purification And Characterization ◽  
Pituitary Glands ◽  
Stimulating Hormone

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.

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.

Purification and Characterization of Glutathione Transferases from the Sea Bass (Dicentrarchus labrax) Liver

2000 ◽  
Vol 373 (2) ◽  
pp. 435-441 ◽  
Author(s):  
Stefania Angelucci ◽  
Paolo Sacchetta ◽  
Pasquale Moio ◽  
Sonia Melino ◽  
Raffaele Petruzzelli ◽  
...  
Keyword(s):  
Dicentrarchus Labrax ◽  
Sea Bass ◽  
Glutathione Transferases ◽  
Purification And Characterization

Purification and Characterization of Recombinant Human Follicle Stimulating Hormone

1992 ◽  
pp. 335-338
Author(s):  
Glenn M. Smith ◽  
Leonora A. Bishop ◽  
Robert DeKroon ◽  
Greg Wright ◽  
Anne Cerpa-Poljak ◽  
...  
Keyword(s):  
Follicle Stimulating Hormone ◽  
Purification And Characterization ◽  
Stimulating Hormone
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