Isolation and characterization of specific rat epididymal proteins

The partial purification and characterization of specific rat epididymal proteins (SEP) is reported. Starting from the cytosol fraction obtained from epididymal homogenates, protein C was purified 15-fold and proteins D-E were purified 19-fold. The molecular weight, determined by molecular sieving,...

Descripción completa

Guardado en:
Detalles Bibliográficos
Publicado: 1979
Materias:
sperm maturation
glycoprotein
protein
animal
article
epididymis
immunodiffusion
isoelectric focusing
male
molecular weight
rat
Animal
Epididymis
Glycoproteins
Immunodiffusion
Isoelectric Focusing
Male
Molecular Weight
Proteins
Rats
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03037207_v13_n1_p73_Garberi
http://hdl.handle.net/20.500.12110/paper_03037207_v13_n1_p73_Garberi
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_03037207_v13_n1_p73_Garberi
record_format dspace
spelling paper:paper_03037207_v13_n1_p73_Garberi2023-06-08T15:28:59Z Isolation and characterization of specific rat epididymal proteins sperm maturation glycoprotein protein animal article epididymis immunodiffusion isoelectric focusing male molecular weight rat Animal Epididymis Glycoproteins Immunodiffusion Isoelectric Focusing Male Molecular Weight Proteins Rats The partial purification and characterization of specific rat epididymal proteins (SEP) is reported. Starting from the cytosol fraction obtained from epididymal homogenates, protein C was purified 15-fold and proteins D-E were purified 19-fold. The molecular weight, determined by molecular sieving, of protein C was 22 400 while that of D-E was 37 000. These proteins stained as glycoproteins with periodic acid-Schiff reagent. The isoelectric point of protein D was 5.13 while that of protein E was 4.95. Protein C separated into 3 bands during isoelectric focussing. The major component focussed at 5.56 and the two minor components at pH 5.38 and 5.79. Using a specific antiserum we could confirm the organ specificity of SEP and their androgen-dependence. © 1979. 1979 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03037207_v13_n1_p73_Garberi http://hdl.handle.net/20.500.12110/paper_03037207_v13_n1_p73_Garberi
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic sperm maturation
glycoprotein
protein
animal
article
epididymis
immunodiffusion
isoelectric focusing
male
molecular weight
rat
Animal
Epididymis
Glycoproteins
Immunodiffusion
Isoelectric Focusing
Male
Molecular Weight
Proteins
Rats
spellingShingle sperm maturation
glycoprotein
protein
animal
article
epididymis
immunodiffusion
isoelectric focusing
male
molecular weight
rat
Animal
Epididymis
Glycoproteins
Immunodiffusion
Isoelectric Focusing
Male
Molecular Weight
Proteins
Rats
Isolation and characterization of specific rat epididymal proteins
topic_facet sperm maturation
glycoprotein
protein
animal
article
epididymis
immunodiffusion
isoelectric focusing
male
molecular weight
rat
Animal
Epididymis
Glycoproteins
Immunodiffusion
Isoelectric Focusing
Male
Molecular Weight
Proteins
Rats
description The partial purification and characterization of specific rat epididymal proteins (SEP) is reported. Starting from the cytosol fraction obtained from epididymal homogenates, protein C was purified 15-fold and proteins D-E were purified 19-fold. The molecular weight, determined by molecular sieving, of protein C was 22 400 while that of D-E was 37 000. These proteins stained as glycoproteins with periodic acid-Schiff reagent. The isoelectric point of protein D was 5.13 while that of protein E was 4.95. Protein C separated into 3 bands during isoelectric focussing. The major component focussed at 5.56 and the two minor components at pH 5.38 and 5.79. Using a specific antiserum we could confirm the organ specificity of SEP and their androgen-dependence. © 1979.
title Isolation and characterization of specific rat epididymal proteins
title_short Isolation and characterization of specific rat epididymal proteins
title_full Isolation and characterization of specific rat epididymal proteins
title_fullStr Isolation and characterization of specific rat epididymal proteins
title_full_unstemmed Isolation and characterization of specific rat epididymal proteins
title_sort isolation and characterization of specific rat epididymal proteins
publishDate 1979
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03037207_v13_n1_p73_Garberi
http://hdl.handle.net/20.500.12110/paper_03037207_v13_n1_p73_Garberi
_version_ 1768542987513495552

Ejemplares similares