Changes in membrane lipids and amino acid transport in a nystatin-resistant Aspergillus niger

1990 ◽  
Vol 36 (6) ◽  
pp. 435-437 ◽  
Author(s):  
Chitra Mazumder ◽  
Joyoti Basu ◽  
Manikuntala Kundu ◽  
Parul Chakrabarti

A nystatin-resistant mutant of Aspergillus niger is described that has quantitative changes in phospholipid composition compared with the wild type. The proportion of linoleic acid in total phospholipids was elevated in the mutant from 38 to 56% and the proportion of oleic acid was lowered from 28 to 12%. Amino acid transport is also altered, the Vmax values for the uptake of leucine, lysine, and glutamic acid being generally higher in the mutant; for glutamic acid the increase was from 15 to 35 nmol∙mg−1∙min−1. Key words: Aspergillus niger, nystatin resistance, phospholipid composition, amino acid transport.

Lipids ◽  
1987 ◽  
Vol 22 (9) ◽  
pp. 609-612 ◽  
Author(s):  
Chitra Mazumder ◽  
Manikuntala Kundu ◽  
Joyoti Basu ◽  
Parul Chakrabarti

Parasitology ◽  
1987 ◽  
Vol 95 (1) ◽  
pp. 71-78 ◽  
Author(s):  
S. A. Jeffs ◽  
C. Arme

SUMMARYProtoscoleces ofEchinococcus granulosusabsorb the l-amino acids proline, methionine, leucine, alanine, serine, phenylalanine, lysine and glutamic acid by a combination of mediated transport and diffusion. All eight amino acids were accumulated against a concentration gradient. Comparison ofKtandVmaxvalues suggests that a low affinity for a particular compound is compensated for by a relatively larger number of transport sites for that compound. Four systems serve for the transport of the eight substrates studied: 2 for neutral (EgNl, EgN2) and 1 each for acidic (EgA) and basic (EgB) amino acids. All eight amino acids are incorporated into protein to varying degrees and substantial portions of absorbed l-alanine and l-methionine are metabolized into other compounds.


1989 ◽  
Vol 143 (1) ◽  
pp. 87-100
Author(s):  
GIORGIO M. HANOZET ◽  
BARBARA GIORDANA ◽  
V. FRANCA SACCHI ◽  
PAOLO PARENTI

The presence of different potassium-dependent amino acid transport systems in the luminal membrane of the larval midgut of Philosamia cynthia Drury (Saturnidae, Lepidoptera) was investigated by means of countertransport experiments performed with brush-border membrane vesicles. The vesicles were preloaded with 14 different unlabelled amino acids, whose ability to elicit an intravesicular accumulation over the equilibrium value of six labelled amino acids (L-alanine, L-leucine, L-phenylalanine, L-glutamic acid, L-lysine and L-histidine) was tested. For histidine, the results were compared with those obtained from inhibition experiments, in which the same 14 amino acids were used as inhibitors on the cis side of the brush-border membrane. The data demonstrate the presence in the lepidopteran luminal membrane of distinct transport pathways for lysine and glutamic acid. The transport of most neutral amino acids, with the exclusionof glycine and proline, seems to occur through a system that may be similar to the neutral brush-border system (NBB) found in mammalian intestinal membranes. This system is also able to handle histidine.


2008 ◽  
Vol 68 (S 01) ◽  
Author(s):  
FM von Versen-Höynck ◽  
A Rajakumar ◽  
JM Roberts ◽  
W Rath ◽  
RW Powers

1976 ◽  
Vol 251 (10) ◽  
pp. 3014-3020 ◽  
Author(s):  
R F Kletzien ◽  
M W Pariza ◽  
J E Becker ◽  
V R Potter ◽  
F R Butcher

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