title: Changes in the activity of soluble arylsulphatase during the post-hatch development and regression after light reduction of Japanese quail testes and epididymides.
abstract: This study demonstrates that specific activity of soluble arylsulphatase (AS) during post-hatch development of Japanese quail testes is the highest for testes weighing from 20 to 200mg, and then decreases as the weight of testes increases, while AS activity per g of wet tissue decreases steadily for testes weighing over 20 to 30 mg. Total AS activity showed a steady increase with the increasing weight of testes. The highest increments in the enzyme activity concerned testes weighing up to 30 mg and those weighing from 30 to 150 mg. Mature animals with testes weighing from 2 to 4 g showed an equal level of total AS activity. Based on this data it is suggested that the changes found in the enzyme activity concern mainly arylsulphatase from Sertoli cells. Specific activity of AS in epididymides remains low until testes reach a weight of approximately 1g and then increases, reaching maximal values for epididymides from the testes of sexually mature animals. Testicular and epididymal regression induced by a short photoperiod (6L:18D) after 30 days of the experiment increases AS activity in the testes and reduces its activity in the epididymides to the values found in the early stages of development. Testes and epididymides in the earliest stage of post-hatch development are characterized by an elution profile of AS in which the form of the enzyme bound to the strong anion exchanger at pH 6.0 is predominant, while in mature animals the form of the enzyme unbound to the anion exchanger predominates in the testes and epididymides. After 30-day regression of the testes and epididymides, the form bound to the anion exchanger did not increase, which suggests that the organs do not return exactly to the stage before sexual maturity.
authors.affiliation: Department of Basic Natural Sciences of Agriculture, University of Rzeszów, Cwiklińskiej str. No. 2, 35-601 Rzeszów, Poland. mdroba@univ.rzeszow.pl
authors.forename: M
authors.initials: M
authors.lastname: Droba
authors.forename: R
authors.initials: R
authors.lastname: Józefczyk
authors.forename: B
authors.initials: B
authors.lastname: Droba
authors.forename: A
authors.initials: A
authors.lastname: Witkowski
mesh_terms: D000818:Animals; D001192:Arylsulfatases / Q000378:metabolism*; D003370:Coturnix / Q000378:metabolism / Q000502:physiology*; D004822:Epididymis / Q000033:anatomy & histology / Q000201:enzymology; D008297:Male; D009929:Organ Size / Q000502:physiology; D017440:Photoperiod; D012708:Sertoli Cells / Q000201:enzymology; D012741:Sexual Maturation / Q000502:physiology*; D013737:Testis / Q000033:anatomy & histology / Q000201:enzymology*
chemical_list: D001192:Arylsulfatases