Wide distribution of pH-dependent service of transport system ASC for both anionic and zwitterionic amino acids

• Published in: The Journal of biological chemistry Vol. 259; no. 6; pp. 3648 - 3652
• Main Authors: Vadgama, J V, Christensen, H N
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Elsevier Inc 25.03.1984; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acids - metabolism; Analytical, structural and metabolic biochemistry; Animals; Binding and carrier proteins; Biological and medical sciences; Biological Transport; Carcinoma, Ehrlich Tumor - metabolism; Cell Line; Columbidae; Cricetinae; Cricetulus; Cysteine - analogs & derivatives; Cysteine - metabolism; Erythrocytes - metabolism; Female; Fundamental and applied biological sciences. Psychology; Humans; Hydrogen-Ion Concentration; Kinetics; Mice; Neurotransmitter Agents; Ovary; Proteins; Sodium - pharmacology; Threonine - metabolism; Human; Cell culture; Transportation system; Rodentia; Red blood cell; Ehrlich ascite cell; Vertebrata; Mammalia; Protonated form; Aminoacid; PH; Aves; CHO-Cell; Comparative study; Hamster; Deprotonation
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(17)43144-9

Criteria have been set up for recognizing the trait of interconvertibility of transport System ASC, whereby it operates in a deprotonated form to mediate the transport of zwitterionic amino acids and in a protonated form to transport anionic amino acids. This trait has been detected by each criterion applied, in all the tested occurrences of System ASC, as follows: the Ehrlich ascites tumor cell in suspension; a cultured variant thereof in monolayer; the Chinese hamster ovary cell CHO-K1 in monolayer; the pigeon red blood cell in suspension; and the human red blood cell in suspension. We conclude that this trait is a general feature of System ASC which may we may use provisionally in defining the system.