Literature DB >> 3956158

Lactate dehydrogenase X, malate dehydrogenase and total protein in rat spermatozoa during epididymal transit.

N T Vermouth, C S Carriazo, R H Ponce, A Blanco.   

Abstract

Lactate dehydrogenase isozyme X (LDH X), malate dehydrogenase (MDH) and total soluble protein have been determined in lysates of spermatozoa isolated from caput, corpus and cauda of rat epididymis. Transit of spermatozoa through epididymis is accompanied by a reduction of LDH X, MDH and total protein per cell in sexually rested animals. The profiles of reduction along epididymal segments are different for the three variables studied. Mating with receptive females during the 5 days prior to determinations increases significantly the levels of MDH in spermatozoa from all sections of epididymis and produces increase of total soluble protein in the cells contained in cauda.

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Year:  1986        PMID: 3956158     DOI: 10.1016/0305-0491(86)90384-6

Source DB:  PubMed          Journal:  Comp Biochem Physiol B        ISSN: 0305-0491


  1 in total

1.  Subcellular localization of branched-chain amino acid aminotransferase and lactate dehydrogenase C4 in rat and mouse spermatozoa.

Authors:  E E Montamat; N T Vermouth; A Blanco
Journal:  Biochem J       Date:  1988-11-01       Impact factor: 3.857

  1 in total

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