&lt;i&gt;&amp;alpha;&lt;/i&gt;-&lt;i&gt;L&lt;/i&gt;-Fucosidase Polymorphism in Human Semen, Blood, and Vaginal Fluid

Gill, Peter; Sutton, J.G.

doi:10.1159/000153469

Cited by 12 publications

(2 citation statements)

References 5 publications

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“…Eiberg et al [1984], Kompf and Ritter [1983] and Olaisen et al [1983] for FI3A, and Gill and Sutton [1984] and Kompf and Ritter [1983] for FUCAI. Tables 2 and 3 summarize the results of the formal analysis undertaken on mother/child pairs, and tables 4 and 5 present data on familial segregation.…”

Section: Resultsmentioning

confidence: 99%

Formal and Population Genetics of F13A and FUCAl Polymorphisms in Northern Portugal

Praia

Amorim²

1990

Hum Hered

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Subunit A of coagulation factor XIII (F13A) and α-L-fucosidase (FUCAl) polymorphisms were studied in unrelated healthy blood donors from northern Portugal. The gene frequencies found were: F13A*2 = 0.241 and FUCA1*2 = 0.308. Segregation analysis in mother/child pairs and nuclear families confirmed the previously described modes of inheritance for F13A and FUCAl, and no evidence for silent genes was found.

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Section: Resultsmentioning

confidence: 99%

Formal and Population Genetics of F13A and FUCAl Polymorphisms in Northern Portugal

Praia

Amorim²

1990

Hum Hered

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“…(EC 3.2.1.51). Previously a-L-fucosidase has been purified from epididymal tissue (Carlsen & Pierce, 1972) and the polymorphism of the enzyme has been identified in human semen (Gill & Sutton, 1984). Recently, Srivastava et al (1986) purified a-L-fucosidase from bovine seminal plasma and demonstrated its role in the acrosome reaction of spermatozoa.…”

Section: Fractionmentioning

confidence: 99%

Hydrolases from bovine seminal vesicle, prostate and Cowper's gland: Hydrolasen aus der Bläschendrüse, Prostata und Cowperschen Drüse des Bullen

2009

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The bovine seminal plasma is formed mainly by secretions of epididymis and the glandular epithelia in ampulla, seminal vesicles, prostate and Cowper's glands. The contribution of each organ to the hydrolytic enzyme activities (glycosidases, exopeptidases, phospholipases) of the bull seminal plasma has been analyzed and is reviewed in this paper with special emphasis on the role of the accessory glands. Seminal vesicles seem to have a major role in the secretion of seminal. plasma acid a-glucosidase, acid a-mannosidase and P-N-acetylhexosaminidase, aminopeptidase A, dipeptidyl peptidase I1 and IV and y-glutamyl transpeptidase as well as Ca2+-dependent and Ca2+-independent phospholipases A, with distinct substrate specificities, a choline-specific phospholipase C and a Co2+ (Mn2+)-activated sphingomyelinase. The enzyme pattern in the ampulla closely resembled that of the seminal vesicles and obviously contributes to the seminal plasma level of these hydrolases. The bull prostate and Cowper's glands contained a strong CaZ+dependent phospholipase A, activity. However, these glands may not contribute to the seminal plasma PLA, activity. At ejaculation the epididymal spermatozoa are exposed to these enzymes. They may have a specific affinity to sugar, peptide or phospholipid residues at distinct sites of the sperm surface. These enzymes may also participate in the digestion of various other semen components to create a suitable milieu for the emitted spermatozoa.Zusammmenfassung. Das Seminalplasma des Bullen wird hauptsachlich von den Sekreten des Nebenhodens und der Driisenepithelien der Ampulle, Blaschendruse, Prostata und Cowperschen Druse gebildet. Der Beitrag eines jeden Organs zu den hydrolytischen Enzymaktivitaten (Glycosidasen, Exopeptidasen, Phospholipasen) des Bullen-Seminalplasmas wurde analysiert und in diesem Ubersichtsartikel besonders im Hinblick auf die Rolle der akzessorischen Geschlechtsdriisen dargestellt. Die Blaschendrusen haben offensichtlich eine groRere Bedeutung fur das Seminalplasma bei der Sekretion der a-Glucosidase, sauren a-Mannosidase und P-N-Acetylhexosaminidase, Aminopeptidase A, Dipeptidylpeptidase I1 und IV und der y-Glutamyltranspeptidase sosie CaZ+-abhangigen und Ca2+-unabhangigen Phospholipasen A, mit verschiedenen Substratspezifizitaten einer Cholin-spezifischen Phospholipase C und einer Co2+ (Mn2+)-aktivierten Sphingomyelinase. Das Enzymmuster der Ampulle ahnelt dem der Blaschendriise sehr stark und tragt Hydrolases in bull accessory glands 11 offensichtlich zum Seminalplasmaspiegel dieser Hydrolasen bei. Die Bullenprostata und Cowpersche Druse enthalten eine starke Ca2+-abhangige Phospholipase A,-Aktivitat. Diese Drusen scheinen jedoch nichts zur PLA,-Aktivitat des Seminalplasmas beizutragen. Bei der Ejakulation werden die Nebenhodenspermien diesen Enzymen ausgesetzt. Sie durften eine spezifische Affinitat fur Zucker, Peptide oder Phospholipidreste an bestimmten Domanen der Spermienoberflache besitzen. AuSerdem konnten diese Enzyme bei der Zerlegung verschiedener anderer Kompone...

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Subtyping of group specific component (GC) in human semen, blood and vaginal fluid by isoelectric focusing in immobilized ph gradients

Pötsch-Schneider

Klein

1988

Electrophoresis

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The group specific component (GC) is stable and well suited for forensic casework. Isoelectric focusing of common GC variants from semen, seminal fluid, vaginal fluid and semen stains, on Immobiline DryPlates, pH 4.5-5.4, is of practical value in criminal investigations of sexual deliquencies. GC is present in normospermia and azoospermia seminal fluids and found in about 20% of the vaginal secretions. The GC patterns observed were similar and in accordance with the bands of the individual GC type in plasma/serum.

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<i>α</i>-<i>L</i>-Fucosidase Polymorphism in Human Semen, Blood, and Vaginal Fluid

Cited by 12 publications

References 5 publications

Formal and Population Genetics of F13A and FUCAl Polymorphisms in Northern Portugal

Formal and Population Genetics of F13A and FUCAl Polymorphisms in Northern Portugal

Hydrolases from bovine seminal vesicle, prostate and Cowper's gland: Hydrolasen aus der Bläschendrüse, Prostata und Cowperschen Drüse des Bullen

Subtyping of group specific component (GC) in human semen, blood and vaginal fluid by isoelectric focusing in immobilized ph gradients

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