Amino acid sequence of myosin essential light chain from the scallop Aquipecten irradians

Biochemistry ◽  
1986 ◽  
Vol 25 (23) ◽  
pp. 7651-7656 ◽  
Author(s):  
John H. Collins ◽  
John Kendrick-Jones ◽  
Ross Jakes ◽  
John Leszyk ◽  
Winifred Barouch ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Essential Light Chain

Amino Acid Sequence of the Essential Light Chain of Adductor Muscle Myosin from Ezo Giant Scallop, Patinopecten yessoensis1

1987 ◽  
Vol 102 (5) ◽  
pp. 1141-1149 ◽  
Author(s):  
Tetsuo MAITA ◽  
Kunihiko KONNO ◽  
Shinsaku MARUTA ◽  
Hajime NORISUE ◽  
Genji MATSUDA
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Adductor Muscle ◽  
Essential Light Chain ◽  
Muscle Myosin

scholarly journals Dictyostelium discoideum myosin: isolation and characterization of cDNAs encoding the essential light chain.

1988 ◽  
Vol 8 (2) ◽  
pp. 794-801 ◽  
Author(s):  
R L Chisholm ◽  
A M Rushforth ◽  
R S Pollenz ◽  
E R Kuczmarski ◽  
S R Tafuri
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Dictyostelium Discoideum ◽  
Light Chain ◽  
Single Gene ◽  
Cdna Expression Library ◽  
Cdna Clones ◽  
Expression Library ◽  
Essential Light Chain ◽  
Isolation And Characterization

We used an antibody specific for Dictyostelium discoideum myosin to screen a lambda gt11 cDNA expression library to obtain cDNA clones which encode the Dictyostelium essential myosin light chain (EMLC). The amino acid sequence predicted from the sequence of the cDNA clone showed 31.5% identity with the amino acid sequence of the chicken EMLC. Comparisons of the Dictyostelium EMLC, a nonmuscle cell type, with EMLC sequences from similar MLCs of skeletal- and smooth-muscle origin, showed distinct regions of homology. Much of the observed homology was localized to regions corresponding to consensus Ca2+-binding of E-F hand domains. Southern blot analysis suggested that the Dictyostelium genome contains a single gene encoding the EMLC. Examination of the pattern of EMLC mRNA expression showed that a significant increase in EMLC message levels occurred during the first few hours of development, coinciding with increased actin expression and immediately preceding the period of maximal chemotactic activity.

Dictyostelium discoideum myosin: isolation and characterization of cDNAs encoding the essential light chain

1988 ◽  
Vol 8 (2) ◽  
pp. 794-801
Author(s):  
R L Chisholm ◽  
A M Rushforth ◽  
R S Pollenz ◽  
E R Kuczmarski ◽  
S R Tafuri
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Dictyostelium Discoideum ◽  
Light Chain ◽  
Single Gene ◽  
Cdna Expression Library ◽  
Cdna Clones ◽  
Expression Library ◽  
Essential Light Chain ◽  
Isolation And Characterization

We used an antibody specific for Dictyostelium discoideum myosin to screen a lambda gt11 cDNA expression library to obtain cDNA clones which encode the Dictyostelium essential myosin light chain (EMLC). The amino acid sequence predicted from the sequence of the cDNA clone showed 31.5% identity with the amino acid sequence of the chicken EMLC. Comparisons of the Dictyostelium EMLC, a nonmuscle cell type, with EMLC sequences from similar MLCs of skeletal- and smooth-muscle origin, showed distinct regions of homology. Much of the observed homology was localized to regions corresponding to consensus Ca2+-binding of E-F hand domains. Southern blot analysis suggested that the Dictyostelium genome contains a single gene encoding the EMLC. Examination of the pattern of EMLC mRNA expression showed that a significant increase in EMLC message levels occurred during the first few hours of development, coinciding with increased actin expression and immediately preceding the period of maximal chemotactic activity.

scholarly journals Amino acid sequence of the light chain of bovine protein C.

1982 ◽  
Vol 257 (20) ◽  
pp. 12170-12179 ◽  
Author(s):  
P Fernlund ◽  
J Stenflo
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Protein C

scholarly journals The amino acid sequence of a lamba light chain presenting abnormal physicochemical and antigenic features

1985 ◽  
Vol 150 (2) ◽  
pp. 349-357 ◽  
Author(s):  
Edith MIHAESCO ◽  
Jean-Pierre ROY ◽  
Nicole CONGY ◽  
Liliane PERAN-RIVAT ◽  
Constantin MIHAESCO
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain

Amino Acid Sequence of the Light Chain of Human Low Molecular Mass Kininogen

1986 ◽  
pp. 91-95
Author(s):  
Friedrich Lottspeich ◽  
Josef Kellermann ◽  
Agnes Henschen ◽  
Günther Rauth ◽  
Werner Müller-Esterl
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Mass ◽  
Light Chain

scholarly journals Arrangement of the disulphide bridges in human low-Mr kininogen

1987 ◽  
Vol 247 (1) ◽  
pp. 15-21 ◽  
Author(s):  
J Kellermann ◽  
C Thelen ◽  
F Lottspeich ◽  
A Henschen ◽  
R Vogel ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Heavy Chain ◽  
Light Chain ◽  
The Other ◽  
Critical Importance

The arrangement of the disulphide bridges in human low-Mr kininogen has been elucidated. Low-Mr kininogen contains 18 half-cystine residues forming nine disulphide bridges. The first and the last half-cystine residues of the amino acid sequence form a disulphide loop which spans the heavy- and the light-chain portion of the kininogen molecule. The other 16 half-cystine residues are linked consecutively to form eight loops of 4-20 amino acids; these loops are lined up in the heavy-chain portion of the kininogen molecule. In this way, a particular pattern of disulphide loops is formed which seems to be of critical importance for the inhibitor function of human kininogen.

Sign in / Sign up

Export Citation Format

Share Document