Pituitary gonadotropic hormone from a chondrostean fish, starred sturgeon (Acipenser stellatus Pall.) III. Polymorphism.
Identifieur interne : 000832 ( Ncbi/Checkpoint ); précédent : 000831; suivant : 000833Pituitary gonadotropic hormone from a chondrostean fish, starred sturgeon (Acipenser stellatus Pall.) III. Polymorphism.
Auteurs : A A Kuznetzov ; B F Goncharov ; E. Burzawa-GerardSource :
- 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.
PubMed: 6840529
Affiliations:
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pubmed:6840529Le document en format XML
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<author><name sortKey="Goncharov, B F" sort="Goncharov, B F" uniqKey="Goncharov B" first="B F" last="Goncharov">B F Goncharov</name>
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<author><name sortKey="Burzawa Gerard, E" sort="Burzawa Gerard, E" uniqKey="Burzawa Gerard E" first="E" last="Burzawa-Gerard">E. Burzawa-Gerard</name>
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<term>Chromatography, Gel</term>
<term>Electrophoresis, Polyacrylamide Gel</term>
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<keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Oocytes</term>
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<term>Biological Assay</term>
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<term>Chromatography, Gel</term>
<term>Electrophoresis, Polyacrylamide Gel</term>
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<front><div type="abstract" xml:lang="en">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.</div>
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