Seminal plasma neutral alpha‐glucosidase activity as an early predictor of patency and natural pregnancy after microsurgical vasoepididymostomy

Andrologia ◽  
2019 ◽  
Vol 51 (5) ◽  
pp. e13235
Author(s):  
Jing‐Ping Li ◽  
Xin‐Zong Zhang ◽  
Jing‐Gen Wu ◽  
Zhong‐Yan Liang ◽  
Yong‐Hong Tian ◽  
...  
Keyword(s):  
Seminal Plasma ◽  
Glucosidase Activity ◽  
Alpha Glucosidase ◽  
Early Predictor

scholarly journals Seminal plasma alpha-glucosidase activity and male infertility

1998 ◽  
Vol 13 (3) ◽  
pp. 591-595 ◽  
Author(s):  
A. M. Mahmoud ◽  
J. Geslevich ◽  
J. Kint ◽  
C. Depuydt ◽  
L. Huysse ◽  
...  
Keyword(s):  
Male Infertility ◽  
Seminal Plasma ◽  
Glucosidase Activity ◽  
Alpha Glucosidase

Seminal Plasma Levels of Neutral Alpha Glucosidase Activity and Its Interactions with Spermiogram in Nigerian Males

2016 ◽  
Vol 9 (4) ◽  
pp. 1-7 ◽  
Author(s):  
Alfred Azenabor ◽  
Jecinta Ezeafulukwe ◽  
Ayodele Ekun ◽  
Babajide Bamiro
Keyword(s):  
Seminal Plasma ◽  
Plasma Levels ◽  
Glucosidase Activity ◽  
Alpha Glucosidase

Alpha‐glucosidase activity in the rat epididymis under different physiological conditions

1997 ◽  
Vol 20 (2) ◽  
pp. 92-95 ◽  
Author(s):  
N. R. KALLA ◽  
S. KAUR ◽  
N. UJWAL ◽  
U. MEHTA ◽  
H. JOOS ◽  
...  
Keyword(s):  
Physiological Conditions ◽  
Glucosidase Activity ◽  
Rat Epididymis ◽  
Alpha Glucosidase

scholarly journals IN VITRO EFFECT OF TERPENOIDS - RICH EXTRACT OF Momordica charantia ON ALPHA GLUCOSIDASE ACTIVITY

Revista Vitae ◽  
2018 ◽  
Vol 25 (3) ◽  
pp. 148-153 ◽  
Author(s):  
A. B. Sallau ◽  
◽  
R. N. Yakubu ◽  
S. M. Aliyu ◽  
A. Salihu ◽  
...  
Keyword(s):  
Momordica Charantia ◽  
Glucosidase Activity ◽  
Vitro Effect ◽  
Alpha Glucosidase

scholarly journals Inhibition of Alpha-glucosidase Activity by Extracts of Ocimum Species (P06-040-19)

2019 ◽  
Vol 3 (Supplement_1) ◽  
Author(s):  
Suresh Mathews ◽  
Mary Nickles ◽  
Caroline Williams ◽  
Charles Cantrell ◽  
Srinivasa Rao Mentreddy
Keyword(s):  
Fine Particles ◽  
Organic Production ◽  
Glucosidase Activity ◽  
Funding Sources ◽  
Crude Extracts ◽  
Species Analysis ◽  
Ocimum Species ◽  
The Family ◽  
Primary Evaluation ◽  
Alpha Glucosidase

Abstract Objectives Ocimum is a genus of aromatic, annual and perennial herbs and shrubs, in the family Lamiaceae, native in Asia, Africa, South, and Central America. Ocimum includes about 150 species; of which the most well- known and widely used for culinary purposes is O. basilicum (basil). Ocimum species have been reported to exhibit anti-diabetic property. The objective of this study was to analyze Ocimum species for antidiabetic properties and identify compound(s) that may be best associated with its anti-hyperglycemic effects. Methods Sixteen Ocimum accessions consisting of three O.africanum, two O.americanum, four O.basilicum, one O.campechianum, two O.gratissimum, and three O.tenuiflorum accessions were cultivated using organic production system. Leaves were harvested at peak vegetative phase, lyophilized, and ground into fine particles and extracted with aqueous methanol. Results A primary evaluation of phytochemicals demonstrated the presence of eugenol, β-sitosterol, caffeic acid, chicoric acid, luteolin, oleanolic acid, rosmarinic acid, and ursolic acid in Ocimum species. Analysis of the crude extracts of the above 16 Ocimum accessions showed that O.tenuiflorum, O.gratissimum, and O.basilicum inhibited yeast alpha glucosidase activity. Of these, O.tenuiflorum demonstrated comparable IC50 inhibitory concentrations as acarbose, a widely-prescribed anti-diabetic medication. Additionally, further sub-fractionation of crude extracts retained and enhanced the alpha glucosidase inhibitory property, with O.tenuiflorum and O.gratissimum showing maximal inhibitory effects (60%–70% inhibition) that were comparable to acarbose (75% inhibition). Conclusions These studies suggest anti-hyperglycemic potential of O.tenuiflorum and O.gratissimum species. Funding Sources NIFA-USDA.

scholarly journals Inhibitory Compounds of .ALPHA.-Glucosidase Activity from Arctium lappa L.

2005 ◽  
Vol 54 (11) ◽  
pp. 589-594 ◽  
Author(s):  
Mitsuo MIYAZAWA ◽  
Nobuo YAGI ◽  
Katsuya TAGUCHI
Keyword(s):  
Arctium Lappa ◽  
Glucosidase Activity ◽  
Inhibitory Compounds ◽  
Alpha Glucosidase

scholarly journals Subcellular distribution of glycosidases in human polymorphonuclear leucocytes

1978 ◽  
Vol 174 (1) ◽  
pp. 53-59 ◽  
Author(s):  
R F Rest ◽  
M H Cooney ◽  
J K Spitznagel
Keyword(s):  
Subcellular Distribution ◽  
Polymorphonuclear Leucocytes ◽  
Density Gradients ◽  
Glucosidase Activity ◽  
Mitochondrial Fractions ◽  
Specific Granules ◽  
Azurophil Granule ◽  
Alpha Galactosidase ◽  
Beta Glucosidase ◽  
Alpha Glucosidase

The subcellular distribution of nine glycosidases were studied in fractions of homogenized human polymorphonuclear leucocytes (neutrophils) obtained by isopycnic centrifugation through linear sucrose density gradients. The substrates were 4-methylumbelliferyl glycosides. All nine glycosides were hydrolysed by enzymes in neutrophil cytosol fractions, and by enzymes in at least one granule population. alpha-Glucosidase activity sedimented in sucrose density gradients to a point (p = 1.180 g/ml) just above the specific granules, possibly the ‘tertiary’ granule population. The peak corresponding to alpha-glucosidase did not co-sediment with, but considerably overlapped, the peak corresponding to lactoferrin, a marker for specific granules (p = 1.187 g/ml). alpha-Galactosidase activity was found primarily in heavy azurophil granules (p = 1.222 g/ml). alpha-Mannosidase activity was found primarily in light azurophil granules (p = 1.206 g/ml), following the distribution of myeloperoxidase, the commonly used azurophil granule marker. beta-Glucosidase activity was concentrated in mitochondrial fractions (p = 1.160 g/ml). All other glycosidases presented complex distributions, with activities not restricted to one granule class. Granule-associated glycosidase activities were increased 2–38 times when measured in the presence of 0.05% Triton X-100, indicating latency of the enzymes within granules.

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