scholarly journals Amino acid composition analysis of human secondary transport proteins and implications for reliable membrane topology prediction

2016 ◽  
Vol 35 (5) ◽  
pp. 929-949 ◽  
Author(s):  
Massoud Saidijam ◽  
Sonia Azizpour ◽  
Simon G. Patching
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Transport Proteins ◽  
Membrane Topology ◽  
Composition Analysis ◽  
Amino Acid Composition Analysis ◽  
Secondary Transport ◽  
Topology Prediction

scholarly journals Comparative codon and amino acid composition analysis of Tritryps-conspicuous features ofLeishmania major

FEBS Letters ◽  
2007 ◽  
Vol 581 (30) ◽  
pp. 5751-5758 ◽  
Author(s):  
Ipsita Chanda ◽  
Archana Pan ◽  
Sanjoy Kumar Saha ◽  
Chitra Dutta
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Composition Analysis ◽  
Amino Acid Composition Analysis

Glycosylphosphatidylinositol-anchored proteins found in the moss Marchantia polymorpha1

2000 ◽  
Vol 28 (6) ◽  
pp. 589-590
Author(s):  
H. Okuyama ◽  
S. Hagiwara ◽  
T. Okamoto ◽  
K. Kato
Keyword(s):  
Amino Acid ◽  
Suspension Culture ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Myristic Acid ◽  
Secretory Protein ◽  
Marchantia Polymorpha ◽  
Composition Analysis ◽  
Gpi Anchor ◽  
Molar Ratios

A suspension culture of the moss Marchantia polymorpha was incubated with either [3H]-ethanolamine or [3H]myristic acid, precursors of a glycosylphosphatidylinositol (GPI) anchor. By both of these a secretory protein of 47 kDa was consistently labelled. Amino acid composition analysis of the chromatographically purified 47-kDa protein exhibited the occurrence of ethanolamine and glucosamine at approximate molar ratios to protein of 1 and 4, respectively. Thus the secretory 47-kDa protein of M. polymorpha was concluded to be a GPI-anchored protein.

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