Characterization of amino acid transport systems in human placental brush-border membrane vesicles

1987 ◽  
Vol 904 (2) ◽  
pp. 309-318 ◽  
Author(s):  
Yoshiki Kudo ◽  
Kazuo Yamada ◽  
Atsushi Fujiwara ◽  
Takashi Kawasaki
Keyword(s):  
Amino Acid ◽  
Brush Border ◽  
Amino Acid Transport ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Transport Systems ◽  
Acid Transport

scholarly journals Studies of Amino Acid Transport into Brush Border Membrane Vesicles Isolated from Rat Small Intestine

1993 ◽  
Vol 64 (7) ◽  
pp. 700-708
Author(s):  
Kiyoshi TAJIMA ◽  
Ryozo TAKADA ◽  
Toru MORI ◽  
Hisao ITABASHI ◽  
Kei-ichiro SUGIMURA
Keyword(s):  
Small Intestine ◽  
Amino Acid ◽  
Brush Border ◽  
Amino Acid Transport ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Rat Small Intestine ◽  
Acid Transport

scholarly journals Reconstitution and identification of the major Na+-dependent neutral amino acid-transport protein from bovine renal brush-border membrane vesicles

1992 ◽  
Vol 281 (1) ◽  
pp. 95-102 ◽  
Author(s):  
F A Doyle ◽  
J D McGivan
Keyword(s):  
Amino Acid ◽  
Brush Border ◽  
Amino Acid Transport ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Acid Transport ◽  
Transport Activity ◽  
Renal Brush Border Membrane ◽  
Renal Brush Border

Amino acid transport activity from bovine renal brush-border membrane vesicles (BBMV) was reconstituted into phospholipid vesicles composed of phosphatidylcholine/5% stearylamine. Reconstitutable transport activity was enhanced in protein fractions binding to various lectins. When solubilized BBMV were fractionated on peanut lectin, a single protein band of average molecular mass 132 kDa was obtained. When this protein fraction was reconstituted into phospholipid membrane vesicles, amino acid transport activity was obtained with properties similar to those in native BBMV with regard to amino acid specificity, although the cation specificity was different. A monoclonal antibody which reacted with the same protein removed reconstitutable amino acid transport activity from solubilized BBMV. These findings may provide the first identification of a renal amino acid-transporting protein, although confirmation of this identification by other approaches will be required.

Sign in / Sign up

Export Citation Format

Share Document