High-performance liquid chromatography of gliadins from different wheat varieties: Amino acid composition and N-terminal amino acid sequence of components

1987 ◽  
Vol 185 (5) ◽  
pp. 371-378 ◽  
Author(s):  
Herbert Wieser ◽  
Anneliese M�dl ◽  
Werner Seilmeier ◽  
Hans-Dieter Belitz
1987 ◽  
Vol 101 (5) ◽  
pp. 1311-1314 ◽  
Author(s):  
Makio HAYAKAWA ◽  
Kazuhiko HORIGOME ◽  
Ichiro KUDO ◽  
Motowo TOMITA ◽  
Shoshichi NOJIMA ◽  
...  

1980 ◽  
Vol 45 (4) ◽  
pp. 1144-1154 ◽  
Author(s):  
Miroslav Baudyš ◽  
Helena Keilová ◽  
Vladimír Kostka

To determine the primary structure of the C-terminal part of the molecule of chicken pepsinogen the tryptic, chymotryptic and thermolytic digest of the protein were investigated and peptides derived from this region were sought. These peptides permitted the following 21-residue C-terminal sequence to be determined: ...Ile-Arg-Glu-Tyr-Tyr-Val-Ile-Phe-Asp-Arg-Ala-Asn-Asn-Lys-Val-Gly-Leu-Ser-Pro-Leu-Ser.COOH. A comparison of this structure with the C-terminal sequential regions of the other acid proteases shows a high degree of homology between chicken pepsinogen and these proteases (e.g., the degree of homology with respect to hog pepsinogen and calf prochymosin is about 66%). Additional tryptic peptides, derived from the N-terminal part of the zymogen molecule whose amino acid sequence has been reported before, were also obtained in this study. This sequence was extended by two residues using an overlapping peptide. An ancillary result of this study was the isolation of tryptic peptides derived from other regions of the zymogen molecule.


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