Changes in guanylate cyclase activity of human platelets in adp-induced aggregation

1991 ◽  
Vol 111 (2) ◽  
pp. 176-179 ◽  
Author(s):  
Yu. Yu. Chirkov ◽  
N. N. Belushkina ◽  
I. A. Tyshchuk ◽  
I. S. Severina
Keyword(s):  
Guanylate Cyclase ◽  
Human Platelets ◽  
Cyclase Activity ◽  
Guanylate Cyclase Activity ◽  
Induced Aggregation

Sex and age differences in soluble guanylate cyclase activity in human platelets

Life Sciences ◽  
1995 ◽  
Vol 58 (5) ◽  
pp. 415-419 ◽  
Author(s):  
Toshio Michimata ◽  
Makoto Imamura ◽  
Haruo Mizuma ◽  
Masami Murakami ◽  
Tokuji Iriuchijima
Keyword(s):  
Age Differences ◽  
Guanylate Cyclase ◽  
Soluble Guanylate Cyclase ◽  
Human Platelets ◽  
Cyclase Activity ◽  
Guanylate Cyclase Activity ◽  
Sex And Age Differences

Guanylate Cyclase Activity in Normal and Neoplastic Squamous Epithelia from the Upper Aero-Digestive Tract

ORL ◽  
1986 ◽  
Vol 48 (5) ◽  
pp. 265-269
Author(s):  
E.L. Rydell ◽  
K.L. Axelsson ◽  
J. Olofsson ◽  
J.E.S. Wikberg
Keyword(s):  
Digestive Tract ◽  
Guanylate Cyclase ◽  
Cyclase Activity ◽  
Guanylate Cyclase Activity ◽  
Squamous Epithelia

scholarly journals Identification of a novel Arabidopsis thaliana nitric oxide-binding molecule with guanylate cyclase activity in vitro

FEBS Letters ◽  
2011 ◽  
Vol 585 (17) ◽  
pp. 2693-2697 ◽  
Author(s):  
Takalani Mulaudzi ◽  
Ndiko Ludidi ◽  
Oziniel Ruzvidzo ◽  
Monique Morse ◽  
Nicolette Hendricks ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Arabidopsis Thaliana ◽  
Guanylate Cyclase ◽  
Cyclase Activity ◽  
Guanylate Cyclase Activity

scholarly journals Histochemistry of guanylate cyclase activity.

1995 ◽  
Vol 43 (12) ◽  
pp. 1235-1240 ◽  
Author(s):  
S Mehdizadeh ◽  
A O'Farrell ◽  
L Bitensky ◽  
J Weisz ◽  
J Alaghband-Zadeh ◽  
...  
Keyword(s):  
Guanylate Cyclase ◽  
Cyclase Activity ◽  
Lead Ions ◽  
Ammonium Citrate ◽  
Considerable Proportion ◽  
Guanosine Triphosphate ◽  
Guanylate Cyclase Activity ◽  
Metal Capture ◽  
Cryostat Sections ◽  
Sufficient Concentration

Guanylate cyclase liberates pyrophosphate from guanosine triphosphate (GTP). In studies published previously, this phosphate is trapped by lead ions even though it is known that free lead ions inactivate a considerable proportion of this enzymatic activity. To overcome the damaging effects of fixation, this study used fresh cryostat sections stabilized with a sufficient concentration of a collagen-derived polypeptide to ensure no measurable loss of guanylate cyclase activity. To avoid the damaging influence of free lead ions, we used a hidden metal capture reagent, i.e., a complex of lead ammonium citrate/acetate that does not react with GTP but which rapidly forms a precipitate with the pyrophosphate liberated by the enzyme. The lead precipitate is then converted into the colored sulfide which is measured in individual cells by microdensitometry. This system was used to measure guanylate cyclase activity in individual cells in unfixed sections of rat liver.

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