Primary structure of subunit B of the 11S globulin of cotton seeds of variety 108-F. II. Peptides of tryptic hydrolysis at lysine residues

1984 ◽  
Vol 20 (2) ◽  
pp. 203-206
Author(s):  
G. A. Piyakina ◽  
T. S. Yunusov ◽  
�. F. Redina
Keyword(s):  
Primary Structure ◽  
Lysine Residues ◽  
Cotton Seeds ◽  
11S Globulin ◽  
Subunit B ◽  
Tryptic Hydrolysis

The globulins of cotton seeds XVII. Primary structure of the carbohydrate-containing subunit C of the 11S globulin

1978 ◽  
Vol 14 (4) ◽  
pp. 470-471 ◽  
Author(s):  
S. I. Asatov ◽  
É. G. Yadgarov ◽  
T. S. Yunusov ◽  
P. Kh. Yuldashev
Keyword(s):  
Primary Structure ◽  
Subunit C ◽  
Cotton Seeds ◽  
11S Globulin

Subunit II (b') and Not Subunit I (b) of Photosynthetic ATP Synthases is Equivalent to Subunit b of the ATP Synthases from Nonphotosynthetic Eubacteria. Evidence for a New Assignment of b-Type F0 Subunits

1997 ◽  
Vol 52 (11-12) ◽  
pp. 789-798 ◽  
Author(s):  
Hans-Jürgen Tiburzy ◽  
Richard J. Berzborn
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Structural Feature ◽  
Atp Synthase ◽  
Primary Structure ◽  
Structural Features ◽  
Amino Acid Sequences ◽  
E Coli ◽  
Subunit B ◽  
Atp Synthases

Abstract Subunit I of chloroplast ATP synthase is reviewed until now to be equivalent to subunit b of Escherichia coli ATP synthase, whereas subunit II is suggested to be an additional subunit in photosynthetic ATP synthases lacking a counterpart in E. coli. After publication of some sequences of subunits II a revision of this assignment is necessary. Based on the analysis of 51 amino acid sequences of b-type subunits concerning similarities in primary structure, iso­electric point and a discovered discontinuous structural feature, our data provide evidence that chloroplast subunit II (subunit b' of photosynthetic eubacteria) and not chloroplast subunit I (subunit b of photosynthetic eubacteria) is the equivalent of subunit b of nonphoto­ synthetic eubacteria, and therefore does have a counterpart in e.g. E. coli. In consequence, structural features essential for function should be looked for on subunit II (b').

scholarly journals The primary structure of cytoplasmatic aspartate aminotransferase from pig heart muscle tryptic hydrolysis products

FEBS Letters ◽  
1971 ◽  
Vol 12 (4) ◽  
pp. 194-196 ◽  
Author(s):  
Yu.A. Ovchinnikov ◽  
A.A. Kiryushkin ◽  
Ts.A. Egorov ◽  
N.G. Abdulaev ◽  
A.P. Kiselev ◽  
...  
Keyword(s):  
Primary Structure ◽  
Aspartate Aminotransferase ◽  
Heart Muscle ◽  
Hydrolysis Products ◽  
Tryptic Hydrolysis
Sign in / Sign up

Export Citation Format

Share Document