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  • 1
    ISSN: 1432-1424
    Keywords: proteoliposomes ; counterflow ; lactose carrier ; phospholipid requirement ; Escherichia coli ; reconstitution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The lactose carrier was extracted from membranes ofEscherichia coli and transport activity reconstituted in proteoliposomes containing different phospholipids. Two different assays f for carrier activity were utilized: counterflow and membrane potential-driven uptake. Proteoliposomes composed ofE. coli lipid or of 50% phosphatidylethanolamine−50% phosphatidylcholine showed very high transport activity with both assays. On the other hand, proteoliposomes containing asolectin, phosphatilcholine or 25% cholesterol/75% phosphatidylcholine showed good counterflow activity but poor membrane potentialdriven uptake. The discrepancy between the two types of transport activity in the latter group of three lipids is not due to leakiness to protons, size of proteoliposomes, or carrier protein content per proteoliposome. Apparently one function of the carrier molecule shows a broad tolerance for various phospholipids, while a second facet of the membrane protein activity requires very restricted lipid enviroment.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 84 (1985), S. 157-164 
    ISSN: 1432-1424
    Keywords: proline transport ; cation cotransport ; harmaline
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Na+ and Li+ were found to stimulate the transport ofl-proline by cells ofEscherichia coli induced for proline utilization. The gene product of the put P gene is involved in the expression of this transport activity since the put P+ strains CSH 4 and WG 148 show activity and the put P− strain RM 2 fails to show this cation coupled transport. The addition of proline was found to stimulate the uptake of Li+ and of Na+. Attempts to demonstrate proline stimulated H+ uptake were unsuccessful. It is concluded that the proline carrier (coded by the put P gene) is responsible for Na+ (or Li+)-proline cotransport.
    Type of Medium: Electronic Resource
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