scholarly journals Amino acid sequence of the beta-subunit of the follicle-stimulating hormone from equine pituitary glands

1978 ◽  
Vol 253 (15) ◽  
pp. 5363-5368
Author(s):  
Y. Fujiki ◽  
P. Rathnam ◽  
B.B. Saxena
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Follicle Stimulating Hormone ◽  
Beta Subunit ◽  
Pituitary Glands ◽  
Stimulating Hormone

Short Communication: Cloning of the red kangaroo (Macropus rufus) follicle stimulating hormone beta subunit

1998 ◽  
Vol 10 (3) ◽  
pp. 289 ◽  
Author(s):  
Katherine Belov ◽  
Gavan A. Harrison ◽  
Desmond W. Cooper
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Follicle Stimulating Hormone ◽  
Hormonal Control ◽  
Beta Subunit ◽  
Brushtail Possum ◽  
Coding Region ◽  
Red Kangaroo ◽  
Antigenic Sites ◽  
Stimulating Hormone

The cDNA encoding the follicle stimulating hormone beta subunit (FSH-β) was isolated from a red kangaroo pituitary cDNA library by using a porcine probe and the nucleotide sequence for the coding region was determined. The highest degree of deduced amino acid sequence identity (91%) was observed between the red kangaroo and another marsupial, the brushtail possum (Trichosurus vulpecula), followed by eutherian species (76%, 75% and 74%, respectively, for pig, mouse and sheep). Based on the deduced red kangaroo FSH-β amino acid sequence, putative antigenic sites have been identified that may prove useful for studying the hormonal control of reproduction in marsupials.

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.

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