Pituitary gonadotropic hormone from a chondrostean fish, starred sturgeon ( Acipenser stellatus Pall.)
Identifieur interne : 002029 ( Main/Exploration ); précédent : 002028; suivant : 002030Pituitary gonadotropic hormone from a chondrostean fish, starred sturgeon ( Acipenser stellatus Pall.)
Auteurs : A. A. Kuznetzov [Russie] ; B. F. Goncharov [Russie] ; E. Burzawa-Gerard [France]Source :
- General and Comparative Endocrinology [ 0016-6480 ] ; 1983.
English descriptors
- KwdEn :
- Animals, Biological Assay, Bufonidae, Chromatography, DEAE-Cellulose, Chromatography, Gel, Electrophoresis, Polyacrylamide Gel, Female, Fishes (metabolism), Gonadotropins, Pituitary (isolation & purification), Gonadotropins, Pituitary (pharmacology), Isoelectric Focusing, Male, Oocytes (drug effects), Oocytes (growth & development), Pituitary Gland (analysis), Polymorphism, Genetic.
- MESH :
- chemical , isolation & purification : Gonadotropins, Pituitary.
- analysis : Pituitary Gland.
- drug effects : Oocytes.
- growth & development : Oocytes.
- metabolism : Fishes.
- chemical , pharmacology : Gonadotropins, Pituitary.
- Animals, Biological Assay, Bufonidae, Chromatography, DEAE-Cellulose, Chromatography, Gel, Electrophoresis, Polyacrylamide Gel, Female, Isoelectric Focusing, Male, Polymorphism, Genetic.
Abstract
Four biologically active fractions of gonadotropic hormone (aci-GTH-A, -B, -C, -D) were isolated and purified from acetonized pituitaries of the starred sturgeon (Acipenser stellatus Pall.). Their separation was achieved by DEAE-cellulose chromatography. Disc-electrophoresis and especially isoelectric focusing in polyacrylamide gel showed that each fraction contained several components. Not less than 15 different components as a whole with isoelectric points ranging from 4.5 to 7.0 could be counted in four aci-GTH preparations. All these components were active in toad oocyte maturation test. Only two of four preparations (aci-GTH-A and -D) were practically free of common components. All aci-GTH preparations were shown to be homogeneous and identical by molecular weight, sedimentation coefficient, sialic acid content, and some immunological properties. N-terminal amino acid analysis revealed tyrosine and leucine in all aci-GTH preparations, with the only exception of aci-GTH-D that contained an additional polypeptide with N-terminal glycine. No differences in the spectra of aci-GTH isoforms were found when pituitary extract, newly purified or 3 years older hormone preparations were submitted to isoelectric focusing.
Url:
DOI: 10.1016/0016-6480(83)90201-0
Affiliations:
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Their separation was achieved by DEAE-cellulose chromatography. Disc-electrophoresis and especially isoelectric focusing in polyacrylamide gel showed that each fraction contained several components. Not less than 15 different components as a whole with isoelectric points ranging from 4.5 to 7.0 could be counted in four aci-GTH preparations. All these components were active in toad oocyte maturation test. Only two of four preparations (aci-GTH-A and -D) were practically free of common components. All aci-GTH preparations were shown to be homogeneous and identical by molecular weight, sedimentation coefficient, sialic acid content, and some immunological properties. N-terminal amino acid analysis revealed tyrosine and leucine in all aci-GTH preparations, with the only exception of aci-GTH-D that contained an additional polypeptide with N-terminal glycine. 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