A multinuclear nmr relaxation study of the interaction of divalent metal ions with l-aspartic acid

1984 ◽  
Vol 22 (1) ◽  
pp. 33-42 ◽  
Author(s):  
Sadegh Khazaeli ◽  
Ronald E. Viola
2000 ◽  
Vol 2 (10) ◽  
pp. 2425-2428 ◽  
Author(s):  
Flaminia Cesare Marincola ◽  
Mariano Casu ◽  
Giuseppe Saba ◽  
Cesare Manetti ◽  
Adolfo Lai

1978 ◽  
Vol 45 (3) ◽  
pp. 433-444 ◽  
Author(s):  
Alan J. Hillier ◽  
G. Richard Jago

SummaryThe fixation of [14C]bicarbonate into aspartate byStreptococcus lactisC10 was achieved by the combined reactions of pyruvate carboxylase (E.C. 6.4.1.1) and glutamate-oxaloacetate transaminase (E.C. 2.6.1.1). The pyruvate carboxylase fromStr. lactisC10, which was most active at pH 8·0, was activated by the divalent metal ions Mn2+, Mg2+and Co2+, and inhibited by sulphydryl reagents. The enzyme was inhibited non-competitively by aspartic acid and competitively by oxaloacetate.


1991 ◽  
Vol 81 (4) ◽  
pp. 462-466 ◽  
Author(s):  
Maria Fabiana Drincovich ◽  
Alberto A. Iglesias ◽  
Carlos S. Andreo

RSC Advances ◽  
2021 ◽  
Vol 11 (21) ◽  
pp. 12815-12825
Author(s):  
Yajie Wang ◽  
Feihong Meng ◽  
Tong Lu ◽  
Chunyun Wang ◽  
Fei Li

Their is a counteraction between a decrease in the disruptive ability of metal-associated oligomer species and an increase in the quantity of oligomers promoted by the metal binding in the activity of hIAPP induced membrane damage.


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