Epithelial cells isolated from chicken jejunum: An experimental model for the study of the functional properties of amino acid transport system b0,+
Author
dc.contributor.author
Angelo,
Author
dc.contributor.author
Rojas Rojas, S.
Author
dc.contributor.author
Ramírez Ramírez, Andrea
Author
dc.contributor.author
Devés, Rosa
Admission date
dc.date.accessioned
2019-01-29T17:50:56Z
Available date
dc.date.available
2019-01-29T17:50:56Z
Publication date
dc.date.issued
2002
Cita de ítem
dc.identifier.citation
Comparative Biochemistry and Physiology - A Molecular and Integrative Physiology, Volumen 132, Issue 3, 2018, Pages 637-644
Identifier
dc.identifier.issn
10956433
Identifier
dc.identifier.other
10.1016/S1095-6433(02)00106-X
Identifier
dc.identifier.uri
https://repositorio.uchile.cl/handle/2250/163461
Abstract
dc.description.abstract
The transport of lysine has been investigated in epithelial cells isolated from chicken jejunum. The kinetics of lysine transport and the pattern of interaction with zwitterionic amino acids were consistent with system b0,+ activity, the broad-spectrum and Na+-independent amino acid transporter. The half-saturation constant for lysine entry (Km±S.E.) was 0.029±0.002 mM and the flux was not affected significantly by Na+ replacement with choline. Lysine influx was inhibited by L-leucine both in Na+ and choline medium with inhibition constants (Ki±S.E.) 0.068±0.006 mM (in Na+) and 0.065±0.009 mM (in choline). Other inhibitory amino acids (Ki±S.E.) were (mM): L-tyrosine (0.073±0.018), L-methionine (0.15±0.015), L-cystine (0.42±0.04), L-cysteine (1.1±0.07), L-isoleucine (1.1±0.09), L-glutamine (1.8±0.16) and L-valine (2.5±0.13). Lysine exit was trans-accelerated (approx. 20 fold) by 2 mM L-lysine and L-leucine. The flux was resistant to pretreatment of the cells with p-chloromercuriphenylsu