Purification and properties of β-galactosidase from chicken seminal plasma

Droba, M.; Droba, B.

doi:10.1016/0305-0491(87)90156-8

Cited by 7 publications

(12 citation statements)

References 14 publications

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“…As in the present study, β-d-galactosidase activity has been detected in oviducal fluid from hen (Droba and Droba 1987), hamster (Tulsiani et al 1996), sheep and cow (Roberts et al 1975(Roberts et al , 1976. N-Acetyl-lactosamine residues have been demonstrated in oviducal epithelial cells in heifers (Cobo et al 2004) and a galactose-binding protein has been identified in spermatozoa from stallion (Dobrinski et al 1996) and rat (Abdullah and Kierszenbaum 1989).…”

Section: Discussionsupporting

confidence: 83%

“…β-N-Acetyl-glucosaminidase activity has also been described in hen (Droba and Droba 1987), sheep (Roberts et al 1976) and cow (Roberts et al 1975) oviducts. Tulsiani et al (1996) did not observe significant differences in the activity of these enzymes throughout the oestrous cycle in hamsters, whereas Roberts et al (1975Roberts et al ( , 1976) detected higher β-N-acetyl-glucosaminidase activity during dioestrus and pregnancy.…”

Section: Discussionmentioning

confidence: 95%

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Glycosidase determination in bovine oviducal fluid at the follicular and luteal phases of the oestrous cycle

Carrasco

Coy

Sánchez

et al. 2008

Reprod. Fertil. Dev.

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Gamete recognition and binding of spermatozoa to the oviduct are carbohydrate-mediated processes in which several glycosidases are thought to have a role, although this has not been demonstrated unequivocally. Oviducal fluid is the biological milieu in which fertilisation and early embryo development take place, but the enzyme composition of oviducal fluid is largely unknown. The aim of the present study was to determine glycosidase activity and protein content in bovine oviducal fluid (bOF) and the volume of fluid collected per oviduct. Oviducts obtained from a slaughterhouse were classified as either in the follicular or luteal phase on the basis of ovarian luteal morphology. Oviducal fluid was aspirated, centrifuged and the volume determined. Samples were then frozen until assay. Substrates conjugated to 4-methylumbelliferyl were used to screen for the activity of seven glycosidases at pH 7.2. The results indicate that bOF has alpha-l-fucosidase, beta-N-acetyl-glucosaminidase, beta-d-galactosidase, alpha-D-mannosidase and beta-N-acetyl-galactosaminidase activity during both phases of the cycle, with the specific activity of the latter two enzymes being higher during the follicular phase. There was no N-acetyl-neuraminidase or alpha-d-galactosidase activity detected in bOF at either phase of the oestrous cycle at pH 7.2, but activity for both glycosidases was detected at pH 4.4. There were no differences in protein concentration or the volume of bOF collected between the two phases of the cycle. These findings indicate that oviducal fluid exhibits glycosidase activity, with specific variations throughout the oestrous cycle, suggesting that these enzymes play a role in carbohydrate-mediated events.

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Section: Discussionsupporting

confidence: 83%

Section: Discussionmentioning

confidence: 95%

Glycosidase determination in bovine oviducal fluid at the follicular and luteal phases of the oestrous cycle

Carrasco

Coy

Sánchez

et al. 2008

Reprod. Fertil. Dev.

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“…The properties of both are summarised in the Table. There was considerable loss of /^-galactosidase activity from spermatozoa after dialysis of the crude extract and after a first run on Phenyl-Sepharose CL-4B column. Similar effects have been described for seminal plasma /?-galactosidase after dialysis and chromatography on Blue-Sepharose CL-6B (Droba and Droba, 1987), and for fowl liver /^-galactosidase after chromatography on DEAE-cellulose (Javeri and Uhlenbruck, 1984). Dialysis may be responsible for removal of small molecular weight activators of /?-galactosidase (for example, CL~ ions).…”

Section: Discussionsupporting

confidence: 54%

“…The characteristics of /?-galactosidase from fowl spermatozoa show some similarities, but also substantial differences, when compared with the /?-galactosidase purified from fowl seminal plasma (Droba and Droba, 1987). The properties of both are summarised in the Table. There was considerable loss of /^-galactosidase activity from spermatozoa after dialysis of the crude extract and after a first run on Phenyl-Sepharose CL-4B column.…”

Section: Discussionmentioning

confidence: 98%

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Properties of acidβ‐galactosidase from fowl spermatozoa

Droba

1988

British Poultry Science

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1. Two forms, I and II, of beta-galactosidase [EC 3.2.1.23] from fowl spermatozoa were separated by Blue-Sepharose CL-6B chromatography. 2. The two forms of the enzyme yielded different pI values (4.1 and 4.7 for form I and 5.3 for form II). 3. Their gel filtration patterns were also different: form I resolved into two peaks with Mr about 65,000 and 80,000, whereas form II resolved into a single peak with an Mr of about 65,000. 4. Both forms had similar optimum pH, pH stability, thermal stability and Km values. 5. Differences between the characteristics of beta-galactosidase forms from spermatozoa and from seminal plasma suggest that the beta-galactosidases investigated in this study are spermatozoa-specific.

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Acid glycosidases from hen oviduct and egg albumen

Droba

Błędniak

2005

Comparative Biochemistry and Physiology Part B: Biochemistry an

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Purification and properties of β-galactosidase from chicken seminal plasma

Cited by 7 publications

References 14 publications

Glycosidase determination in bovine oviducal fluid at the follicular and luteal phases of the oestrous cycle

Glycosidase determination in bovine oviducal fluid at the follicular and luteal phases of the oestrous cycle

Properties of acidβ‐galactosidase from fowl spermatozoa

Acid glycosidases from hen oviduct and egg albumen

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