Faculty Opinions recommendation of Cu(I)-dependent biogenesis of the galactose oxidase redox cofactor.

Author(s):  
Antonio Rosato
Keyword(s):  

1982 ◽  
Vol 48 (02) ◽  
pp. 211-216 ◽  
Author(s):  
V M Haver ◽  
A R L Gear

SummaryPlatelet heterogeneity has been studied with a technique called functional fractionation which employs gentle centrifugation to yield subpopulations (“reactive” and “less-reactive” platelets) after exposure to small doses of aggregating agent. Aggregation kinetics of the different platelet populations were investigated by quenched-flow aggregometry. The large, “reactive” platelets were more sensitive to ADP (Ka = 1.74 μM) than the smaller “less-reactive” platelets (Ka = 4.08 μM). However, their maximal rate of aggregation (Vmax, % of platelets aggregating per sec) of 23.3 was significantly lower than the “less-reactive” platelets (Vmax = 34.7). The “reactive” platelets had a 2.2 fold higher level of cyclic AMP.Platelet glycoproteins were labeled using the neuraminidase-galactose oxidase – [H3]-NaBH4 technique. When platelets were labeled after reversible aggregation, the “reactive” platelets showed a two-fold decrease in labeling efficiency (versus control platelets). However, examination of whole cells or membrane preparations from reversibly aggregated platelets revealed no significant difference in Coomassie or PAS (Schiff) staining.These results suggest that the large, “reactive” platelets are more sensitive to ADP but are not hyperaggregable in a kinetic sense. Reversible aggregation may cause a re-orientation of membrane glycoproteins that is apparently not characterized by a major loss of glycoprotein material.



1994 ◽  
Vol 269 (40) ◽  
pp. 25095-25105
Author(s):  
A.J. Baron ◽  
C. Stevens ◽  
C. Wilmot ◽  
K.D. Seneviratne ◽  
V. Blakeley ◽  
...  


1978 ◽  
Vol 24 (8) ◽  
pp. 898-903 ◽  
Author(s):  
Geraldine A. Tomlinson ◽  
Maureen P. Strohm ◽  
Lawrence I. Hochstein

Nongrowing cells of Halobacterium saccharovorum oxidized lactose to a product identified as lactobionic acid by thin-layer, paper, and column chromatography, and by identification of the galactose and gluconic acid produced from it after acid hydrolysis. Growing cells oxidized lactose to a product that was identical with lactobionate except that it did not serve as a substrate for galactose oxidase. While the identity of this compound has not been established, it is suggested that the product is lactobionic acid in which the galactose moeity is in the furanose form. Neither lactobionate nor the product produced by growing cells was further metabolized, suggesting that lactose oxidation is not coupled to growth.



2000 ◽  
Vol 8 (1-3) ◽  
pp. 3-15 ◽  
Author(s):  
Mei M. Whittaker ◽  
Christopher A. Ekberg ◽  
James Peterson ◽  
Mariana S. Sendova ◽  
Edmund P. Day ◽  
...  


2004 ◽  
Vol 17 (2) ◽  
pp. 141-148 ◽  
Author(s):  
D. Wilkinson ◽  
N. Akumanyi ◽  
R. Hurtado-Guerrero ◽  
H. Dawkes ◽  
P.F. Knowles ◽  
...  




2001 ◽  
Vol 40 (11) ◽  
pp. 2528-2533 ◽  
Author(s):  
Craig Wright ◽  
A. Geoffrey Sykes
Keyword(s):  


1972 ◽  
Vol 9 (11) ◽  
pp. 1095-1101 ◽  
Author(s):  
Sergio Estrada-Parra ◽  
Irma Gómez


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