The globulins of cotton seeds X. Structures of tryptic peptides of the 7S globulin

1977 ◽  
Vol 13 (5) ◽  
pp. 563-566 ◽  
Author(s):  
É. F. Redina ◽  
M. A. Kuchenkova ◽  
L. G. Petrosyan ◽  
P. Kh. Yuldashev
Keyword(s):  
Tryptic Peptides ◽  
7S Globulin ◽  
Cotton Seeds

A study of the globulins of cotton seeds VI. Peptides of a trytpic hydrolyzate of subunit I of the 7S globulin

1977 ◽  
Vol 13 (4) ◽  
pp. 493-494
Author(s):  
E. F. Redina ◽  
M. A. Kuchenkova ◽  
P. Kh. Yuldashev
Keyword(s):  
7S Globulin ◽  
Cotton Seeds

Investigation of the globulins of cotton seeds VII. Peptides of a triptic hydrolyzate of the 7S-globulin

1977 ◽  
Vol 13 (4) ◽  
pp. 464-467
Author(s):  
É. F. Redina ◽  
M. A. Kuchenkova ◽  
P. Kh. Yuldashev
Keyword(s):  
7S Globulin ◽  
Cotton Seeds

The globulins of cotton seeds XI. The structure of the chymotryptic peptides of the 7S globulin

1977 ◽  
Vol 13 (5) ◽  
pp. 566-569 ◽  
Author(s):  
N. L. Ovchinnikova ◽  
M. A. Kuchenkova ◽  
T. D. Kasymova ◽  
P. Kh. Yuldashev
Keyword(s):  
7S Globulin ◽  
Cotton Seeds

A study of the structure of the 11S globulin from cotton seeds XIV. Tryptic peptides of subunit C

1978 ◽  
Vol 14 (2) ◽  
pp. 231-232
Author(s):  
S. I. Asatov ◽  
T. S. Yunusov ◽  
P. Kh. Yuldashev
Keyword(s):  
Tryptic Peptides ◽  
Subunit C ◽  
Cotton Seeds ◽  
11S Globulin

The globulins of cotton seeds XIX. Chymotryptic and tryptic peptides of subunit C of the 11S globulin

1978 ◽  
Vol 14 (5) ◽  
pp. 526-532
Author(s):  
É. G. Yadgarov ◽  
S. I. Asatov ◽  
T. S. Yunusov ◽  
P. Kh. Yuldashev
Keyword(s):  
Tryptic Peptides ◽  
Subunit C ◽  
Cotton Seeds ◽  
11S Globulin

The globulins of cotton seeds XII. The structure of the 7S-globulin

1977 ◽  
Vol 13 (5) ◽  
pp. 570-572 ◽  
Author(s):  
M. A. Kuchenkova ◽  
É. F. Redina ◽  
N. L. Ovchinnikova ◽  
P. Kh. Yuldashev
Keyword(s):  
7S Globulin ◽  
Cotton Seeds

Warm and freeze-fracture of cotton seed radicles

1987 ◽  
Vol 45 ◽  
pp. 984-985
Author(s):  
E. L. Vigil ◽  
E. F. Erbe
Keyword(s):  
Thin Film ◽  
Water Vapor ◽  
Fracture Surface ◽  
Membrane Structure ◽  
Room Temperature ◽  
Freeze Fracture ◽  
Longitudinal Axis ◽  
Fracture Plane ◽  
Cotton Seeds ◽  
Condensed Water

In cotton seeds the radicle has 12% moisture content which makes it possible to prepare freeze-fracture replicas without fixation or cryoprotection. For this study we have examined replicas of unfixed radicle tissue fractured at room temperature to obtain data on organelle and membrane structure.Excised radicles from seeds of cotton (Gossyplum hirsutum L. M-8) were fractured at room temperature along the longitudinal axis. The fracture was initiated by spliting the basal end of the excised radicle with a razor. This procedure produced a fracture through the tissue along an unknown fracture plane. The warm fractured radicle halves were placed on a thin film of 100% glycerol on a flat brass cap with fracture surface up. The cap was rapidly plunged into liquid nitrogen and transferred to a freeze- etch unit. The sample was etched for 3 min at -95°C to remove any condensed water vapor and then cooled to -150°C for platinum/carbon evaporation.

Molecular identification of a new soybean germplasm Zhonghuang 608 lacking of 7S globulin alpha' subunit

2019 ◽  
Vol 45 (1) ◽  
pp. 18
Author(s):  
Jun-Ying LI ◽  
Ru-Jian SUN ◽  
Zhong-Feng LI ◽  
Zhong-Yan WEI ◽  
Yu-Long REN ◽  
...  
Keyword(s):  
Molecular Identification ◽  
Alpha Subunit ◽  
Soybean Germplasm ◽  
7S Globulin

C-Terminal amino acid sequence of chicken pepsinogen and its homology with sequences of other acid proteases

1980 ◽  
Vol 45 (4) ◽  
pp. 1144-1154 ◽  
Author(s):  
Miroslav Baudyš ◽  
Helena Keilová ◽  
Vladimír Kostka
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
The Other ◽  
Terminal Sequence ◽  
Terminal Part ◽  
Terminal Amino Acid ◽  
Tryptic Peptides ◽  
Terminal Amino ◽  
High Degree ◽  
Terminal Amino Acid Sequence

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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