scholarly journals The complete amino acid sequence of chicken skeletal-muscle enolase

1986 ◽  
Vol 236 (1) ◽  
pp. 115-126 ◽  
Author(s):  
G A Russell ◽  
B Dunbar ◽  
L A Fothergill-Gilmore
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Peptide Bond ◽  
Peptide Bonds ◽  
Complete Amino Acid Sequence ◽  
Arginine Residues ◽  
Cnbr Cleavage ◽  
Yeast Enolase ◽  
Chicken Skeletal Muscle

The complete amino acid sequence of chicken skeletal-muscle enolase, comprising 433 residues, was determined. The sequence was deduced by automated sequencing of hydroxylamine-cleavage, CNBr-cleavage, o-iodosobenzoic acid-cleavage, clostripain-digest and staphylococcal-proteinase-digest fragments. The presence of several acid-labile peptide bonds and the tenacious aggregation of most CNBr-cleavage fragments meant that a commonly used sequencing strategy involving initial CNBr cleavage was unproductive. Cleavage at the single Asn-Gly peptide bond with hydroxylamine proved to be particularly useful. Comparison of the sequence of chicken enolase with the two yeast enolase isoenzyme sequences shows that the enzyme is strongly conserved, with 60% of the residues identical. The histidine and arginine residues implicated as being important for the activity of yeast enolase are conserved in the chicken enzyme. Secondary-structure predictions are analysed in an accompanying paper [Sawyer, Fothergill-Gilmore & Russell (1986) Biochem. J. 236, 127-130].

scholarly journals Completion of the amino acid sequence of the α1 chain from type I calf skin collagen. Amino acid sequence of α1(I)B8

1983 ◽  
Vol 215 (1) ◽  
pp. 183-189 ◽  
Author(s):  
R W Glanville ◽  
D Breitkreutz ◽  
M Meitinger ◽  
P P Fietzek
Keyword(s):  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Type I ◽  
Amino Acid Sequence Analysis ◽  
Complete Amino Acid Sequence ◽  
Skin Collagen ◽  
Arginine Residues ◽  
Calf Skin

The complete amino acid sequence of the 279-residue CNBr peptide CB8 from the alpha 1 chain of type I calf skin collagen is presented. It was determined by sequencing overlapping fragments of CB8 produced by Staphylococcus aureus V8 proteinase, trypsin, Endoproteinase Arg-C and hydroxylamine. Tryptic cleavages were also made specific for lysine by blocking arginine residues with cyclohexane-1,2-dione. This completes the amino acid sequence analysis of the 1054-residues-long alpha (I) chain of calf skin collagen.

scholarly journals Amino acid sequence of the Bb fragment from human complement Factor B. Alignment of the cyanogen bromide-cleavage peptides

1983 ◽  
Vol 209 (1) ◽  
pp. 51-60 ◽  
Author(s):  
J Gagnon ◽  
D L Christie
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Factor ◽  
Alternative Pathway ◽  
Amino Acid Sequences ◽  
Complement Factor ◽  
Factor B ◽  
Arginine Residues ◽  
Alternative Pathway Of Complement ◽  
Cnbr Cleavage

The alignment of all the CNBr-cleavage peptides of fragment Bb from human Factor B (a component of the alternative pathway of complement) was determined. This was derived from cleavage of the fragment Bb at arginine residues by using trypsin and clostripain. Details of the isolation and amino acid sequences of these peptides are given. Together with previously published N-terminal sequences of the CNBr-cleavage peptides [Christie & Gagnon (1982) Biochem. J. 201, 555-567], this provides the amino acid sequence of the N-terminal half of fragment Bb.

scholarly journals Complete Amino-Acid Sequence of Actin of Rabbit Skeletal Muscle

1973 ◽  
Vol 70 (9) ◽  
pp. 2687-2691 ◽  
Author(s):  
M. Elzinga ◽  
J. H. Collins ◽  
W. M. Kuehl ◽  
R. S. Adelstein
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Rabbit Skeletal Muscle ◽  
Complete Amino Acid Sequence

An uncoupling protein homologue putatively involved in facultative muscle thermogenesis in birds

2001 ◽  
Vol 353 (3) ◽  
pp. 441-444 ◽  
Author(s):  
Serge RAIMBAULT ◽  
Sami DRIDI ◽  
Frédérique DENJEAN ◽  
Joël LACHUER ◽  
Elodie COUPLAN ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Uncoupling Protein ◽  
Chicken Line ◽  
Diet Induced Thermogenesis ◽  
Avian Ucp ◽  
Developing Muscle ◽  
Chicken Skeletal Muscle ◽  
Shivering Thermogenesis

The cDNA of an uncoupling protein (UCP) homologue was obtained by screening a chicken skeletal-muscle library. The predicted 307-amino-acid sequence of avian UCP (avUCP) is 55, 70, 70 and 46% identical with mammalian UCP1, UCP2 and UCP3 and plant UCP respectively. avUCP mRNA expression is restricted to skeletal muscle and its abundance was increased 1.3-fold in a chicken line showing diet-induced thermogenesis, and 3.6- and 2.6-fold in cold-acclimated and glucagon-treated ducklings developing muscle non-shivering thermogenesis respectively. The present data support the implication of avUCP in avian energy expenditure.

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