Human leucocyte α-l-fucosidase

Troost, J.; Heijden, M.C.M. van der; Staal, Gerard E.J.

doi:10.1016/0009-8981(76)90179-0

Cited by 17 publications

(2 citation statements)

References 7 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…a-L-Fucosidase has been demon strated in serum, leucocytes, kidney, liver, lung, spleen, placenta and muscle [I, 12] and in purified extracts of urine [10]. This is the first report of a-L-fucosidase polymorphism in semen, although Mann [6] records very high activity in semen for this enzyme.…”

Section: Introductionmentioning

confidence: 91%

See 1 more Smart Citation

α-L-Fucosidase Polymorphism in Human Semen, Blood, and Vaginal Fluid

Gill¹,

Sutton²

1984

Hum Hered

View full text Add to dashboard Cite

The diallelic enzyme α-L-fucosidase has been found to be highly active in semen. Eight distinct enzyme bands were observed in each homozygote and the heterozygote consisted of a combination of bands. The isoelectric points ranged between pI 4.34 and 6.65. Activity was found to be much lower in vaginal fluid, not more than three cathodal bands were visible in any sample examined. In leucocytes, 5 bands were detected in homozygotes whilst in serum only two faint anodal bands could be detected. Activity was low in vaginal fluid and could not be detected in urine or saliva. Population studies were carried out on semen samples from Oxford and Basingstoke and on lymphocyte samples from Oxford. The data were in agreement with Hardy-Weinburg equilibrium. The common allele (Fu 1) had a frequency of 0.704 in Oxford semen samples.

show abstract

Section: Introductionmentioning

confidence: 91%

“…Troost et al [10] have reported the pres ence of a-L-fucosidase in purified urine. However, it was not detected in either sali va or urine during the course of the work reported here.…”

Section: A-l-fucosidase In Saliva and Urinementioning

confidence: 99%

α-L-Fucosidase Polymorphism in Human Semen, Blood, and Vaginal Fluid

Gill¹,

Sutton²

1984

Hum Hered

View full text Add to dashboard Cite

show abstract

Glycosidases—Properties and Application to the Study of Complex Carbohydrates and Cell Surfaces

Flowers¹,

Sharon²

1979

Advances in Enzymology - And Related Areas of Molecular Biology

View full text Add to dashboard Cite

Glycolipid and Glycoprotein Degradation

Conzelmann

Sandhoff

1987

Advances in Enzymology - And Related Areas of Molecular Biology

View full text Add to dashboard Cite

Human leucocyte α-l-fucosidase

Cited by 17 publications

References 7 publications

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

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

Glycosidases—Properties and Application to the Study of Complex Carbohydrates and Cell Surfaces

Glycolipid and Glycoprotein Degradation

Contact Info

Product

Resources

About

Human leucocyte α-l-fucosidase

Cited by 17 publications

References 7 publications

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

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

Glycosidases—Properties and Application to the Study of Complex Carbohydrates and Cell Surfaces

Glycolipid and Glycoprotein Degradation

Contact Info

Product

Resources

About

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

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