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Title:
l-Glutamine transport in native vesicles isolated from Ehrlich ascites tumor cell membranes | Journal of Bioenergetics and Biomembranes
Description:
Native vesicles isolated from Ehrlich ascites tumor cells accumulate glutamine by means of Na+-dependent transport systems; thiocyanate seems to be the more effective anion. The apparent affinity constant for the process was 0.38 mM. The Arrhenius plot gave an apparent activation energy of 12.3 kJ/mol. The structural analogs of glutamine, acivicin (2.5 mM) and azaserine (2.5 mM), inhibited the net uptake by 67 and 70%, respectively. The sulfhydryl reagents mersalyl, PCMBS, NEM, and DTNB also inhibited net uptake, suggesting that sulfhydryl groups may be involved in the activity of the carrier protein. A strong inhibition was detected when the vesicles were incubated in the presence of alanine, cysteine, or serine; in addition, histidine, but not glutamate or leucine, had a negative effect on glutamine transport.
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google, scholar, transport, article, biochem, quesada, castro, johnstone, biol, medina, núñez, glutamine, access, privacy, cookies, content, journal, chem, publish, research, search, vesicles, ehrlich, mccormick, data, information, log, lglutamine, native, isolated, ascites, tumor, cell, ana, uptake, open, discover, cancer, int, van, download, springer, optional, personal, parties, policy, find, track, bioenergetics, biomembranes,
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l-glutamine transport na+-dependent transport systems month download article/chapter glutamine transport núñez de castro related subjects privacy choices/manage cookies full article pdf native vesicles isolated facultad de ciencias check access instant access european economic area apparent affinity constant arrhenius plot gave apparent activation energy universidad de málaga conditions privacy policy sulfhydryl reagents mersalyl accepting optional cookies structural analogs carrier protein de castro journal finder publish main content log article journal inhibited net uptake quesada rights cell growth latest articles article medina article log google scholar article cite glutamine de graaf privacy policy personal data biomembranes aims net uptake activity books a optional cookies manage preferences spain miguel journal publish data protection essential cookies cookies skip subscription content
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headline:l-Glutamine transport in native vesicles isolated from Ehrlich ascites tumor cell membranes
description:Native vesicles isolated from Ehrlich ascites tumor cells accumulate glutamine by means of Na+-dependent transport systems; thiocyanate seems to be the more effective anion. The apparent affinity constant for the process was 0.38 mM. The Arrhenius plot gave an apparent activation energy of 12.3 kJ/mol. The structural analogs of glutamine, acivicin (2.5 mM) and azaserine (2.5 mM), inhibited the net uptake by 67 and 70%, respectively. The sulfhydryl reagents mersalyl, PCMBS, NEM, and DTNB also inhibited net uptake, suggesting that sulfhydryl groups may be involved in the activity of the carrier protein. A strong inhibition was detected when the vesicles were incubated in the presence of alanine, cysteine, or serine; in addition, histidine, but not glutamate or leucine, had a negative effect on glutamine transport.
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l-Glutamine
amino acid transport
plasma membrane vesicle
Ehrlich cells
Bioorganic Chemistry
Biochemistry
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Animal Biochemistry
Organic Chemistry
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headline:l-Glutamine transport in native vesicles isolated from Ehrlich ascites tumor cell membranes
description:Native vesicles isolated from Ehrlich ascites tumor cells accumulate glutamine by means of Na+-dependent transport systems; thiocyanate seems to be the more effective anion. The apparent affinity constant for the process was 0.38 mM. The Arrhenius plot gave an apparent activation energy of 12.3 kJ/mol. The structural analogs of glutamine, acivicin (2.5 mM) and azaserine (2.5 mM), inhibited the net uptake by 67 and 70%, respectively. The sulfhydryl reagents mersalyl, PCMBS, NEM, and DTNB also inhibited net uptake, suggesting that sulfhydryl groups may be involved in the activity of the carrier protein. A strong inhibition was detected when the vesicles were incubated in the presence of alanine, cysteine, or serine; in addition, histidine, but not glutamate or leucine, had a negative effect on glutamine transport.
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pageEnd:697
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amino acid transport
plasma membrane vesicle
Ehrlich cells
Bioorganic Chemistry
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Animal Biochemistry
Organic Chemistry
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