A 11.5-kb 5′-Terminal cDNA Sequence of Chicken Breast Muscle Connectin/Titin Reveals Its Z Line Binding Region

A partial 5′-region cDNA (11.5 kb) of chicken breast muscle connectin/titin encoding 3752 amino acids was sequenced. The predicted amino acid sequence contains 31 immunoglobulin C2 motifs and 10 interdomains. The sequence suggests a skeletal muscle type of connectin isoforms. Immunoelectron microsco...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1996-06, Vol.223 (1), p.160-164
Main Authors: Yajima, Hirohiko, Ohtsuka, Hiroshi, Kawamura, Yuuki, Kume, Hideaki, Murayama, Takashi, Abe, Hiroshi, Kimura, Sumiko, Maruyama, Koscak
Format: Article
Language:English
Subjects:
ADN
Animals
Binding Sites
Carrier Proteins - biosynthesis
Chickens
Cloning, Molecular
COMPOSICION QUIMICA
COMPOSITION CHIMIQUE
Connectin
DNA, Complementary - chemistry
DNA, Complementary - metabolism
Escherichia coli
Gene Library
Glutathione Transferase
Microscopy, Immunoelectron
MUSCLE
Muscle Proteins - biosynthesis
Muscle Proteins - genetics
Muscle Proteins - ultrastructure
Muscle, Skeletal - metabolism
MUSCULOS
Myocardium - metabolism
PEPTIDE
PEPTIDOS
POLLO
POULET
Protein Kinases - biosynthesis
Protein Kinases - genetics
Protein Kinases - ultrastructure
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - metabolism
Recombinant Fusion Proteins - ultrastructure
Sarcomeres - metabolism
Sarcomeres - ultrastructure
TEJIDOS ANIMALES
TISSU ANIMAL
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Description
Summary:A partial 5′-region cDNA (11.5 kb) of chicken breast muscle connectin/titin encoding 3752 amino acids was sequenced. The predicted amino acid sequence contains 31 immunoglobulin C2 motifs and 10 interdomains. The sequence suggests a skeletal muscle type of connectin isoforms. Immunoelectron microscopic studies using antisera raised against several products of the cDNA fragments expressed inE. colirevealed that a region of some 800 amino acids from the N terminus of connectin is involved in its binding to the Z line in a sarcomere.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1996.0862