scholarly journals Isolation and characterization of related cDNA clones encoding skeletal muscle beta-tropomyosin and a low-molecular-weight nonmuscle tropomyosin isoform.

1989 ◽  
Vol 9 (1) ◽  
pp. 185-192 ◽  
Author(s):  
J A Bradac ◽  
C E Gruber ◽  
S Forry-Schaudies ◽  
S H Hughes
Keyword(s):  
Skeletal Muscle ◽  
Molecular Weight ◽  
Amino Acid ◽  
Cdna Library ◽  
Low Molecular Weight ◽  
Cdna Clones ◽  
Protein Coding ◽  
Coding Sequence ◽  
Untranslated Sequence ◽  
Complete Protein

We have isolated and characterized cDNA clones from chicken cDNA libraries derived from skeletal muscle, body wall, and cultured fibroblasts. A clone isolated from a skeletal muscle cDNA library contains the complete protein-coding sequence of the 284-amino-acid skeletal muscle beta-tropomyosin together with 72 bases of 5' untranslated sequence and nearly the entire 3' untranslated region (about 660 bases), lacking only the last 4 bases and the poly(A) tail. A second clone, isolated from the fibroblast cDNA library, contains the complete protein-coding sequence of a 248-amino-acid fibroblast tropomyosin together with 77 bases of 5' untranslated sequence and 235 bases of 3' untranslated sequence through the poly(A) tract. The derived amino acid sequence from this clone exhibits only 82% homology with rat fibroblast tropomyosin 4 and 80% homology with human fibroblast tropomyosin TM30nm, indicating that this clone encodes a third 248-amino-acid tropomyosin isoform class. The protein product of this mRNA is fibroblast tropomyosin 3b, one of two low-molecular-weight isoforms expressed in chicken fibroblast cultures. Comparing the sequences of the skeletal muscle and fibroblast cDNAs with a previously characterized clone which encodes the smooth muscle alpha-tropomyosin reveals two regions of absolute homology, suggesting that these three clones were derived from the same gene by alternative RNA splicing.

Isolation and characterization of related cDNA clones encoding skeletal muscle beta-tropomyosin and a low-molecular-weight nonmuscle tropomyosin isoform

1989 ◽  
Vol 9 (1) ◽  
pp. 185-192
Author(s):  
J A Bradac ◽  
C E Gruber ◽  
S Forry-Schaudies ◽  
S H Hughes
Keyword(s):  
Skeletal Muscle ◽  
Molecular Weight ◽  
Amino Acid ◽  
Cdna Library ◽  
Low Molecular Weight ◽  
Cdna Clones ◽  
Protein Coding ◽  
Coding Sequence ◽  
Untranslated Sequence ◽  
Complete Protein

We have isolated and characterized cDNA clones from chicken cDNA libraries derived from skeletal muscle, body wall, and cultured fibroblasts. A clone isolated from a skeletal muscle cDNA library contains the complete protein-coding sequence of the 284-amino-acid skeletal muscle beta-tropomyosin together with 72 bases of 5' untranslated sequence and nearly the entire 3' untranslated region (about 660 bases), lacking only the last 4 bases and the poly(A) tail. A second clone, isolated from the fibroblast cDNA library, contains the complete protein-coding sequence of a 248-amino-acid fibroblast tropomyosin together with 77 bases of 5' untranslated sequence and 235 bases of 3' untranslated sequence through the poly(A) tract. The derived amino acid sequence from this clone exhibits only 82% homology with rat fibroblast tropomyosin 4 and 80% homology with human fibroblast tropomyosin TM30nm, indicating that this clone encodes a third 248-amino-acid tropomyosin isoform class. The protein product of this mRNA is fibroblast tropomyosin 3b, one of two low-molecular-weight isoforms expressed in chicken fibroblast cultures. Comparing the sequences of the skeletal muscle and fibroblast cDNAs with a previously characterized clone which encodes the smooth muscle alpha-tropomyosin reveals two regions of absolute homology, suggesting that these three clones were derived from the same gene by alternative RNA splicing.

scholarly journals Genome Sequence of a Novel Canine Picornavirus Isolated from an American Foxhound

2017 ◽  
Vol 5 (20) ◽  
Author(s):  
Erica E. Norby ◽  
Richard G. Jarman ◽  
Paul B. Keiser ◽  
Leonard N. Binn ◽  
Jun Hang
Keyword(s):  
Amino Acid ◽  
Genome Sequence ◽  
Canis Lupus ◽  
Canis Lupus Familiaris ◽  
Protein Coding ◽  
Content Type ◽  
Coding Sequence ◽  
Complete Protein

ABSTRACT A candidate new canine picornavirus was isolated from a respiratory swab collected from an American foxhound (Canis lupus familiaris) in 1968. The assembled genome sequence of strain A128thr is 7,618 bases in length, comprising a complete protein-coding sequence of the 2,213-amino-acid polyprotein and partial terminal untranslated sequences.

scholarly journals A phosphorylated light-chain component of myosin from skeletal muscle

1973 ◽  
Vol 135 (1) ◽  
pp. 151-164 ◽  
Author(s):  
W. T. Perrie ◽  
L. B. Smillie ◽  
S. V. Perry
Keyword(s):  
Skeletal Muscle ◽  
Molecular Weight ◽  
Amino Acid ◽  
Light Chain ◽  
Sodium Dodecyl Sulphate ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Low Molecular Weight ◽  
Obvious Similarity

1. The low-molecular-weight components of myosin from rabbit skeletal muscle migrated as four bands on polyacrylamide-gel electrophoresis in 8m-urea but only as three in systems containing sodium dodecyl sulphate. The two bands of intermediate mobility in 8m-urea (Ml2 and Ml3) had identical mobilities in sodium dodecyl sulphate. 2. The isolation of pure samples of all four low-molecular-weight components by DEAE-Sephadex chromatography is described. 3. The amino acid compositions of components Ml2 and Ml3 were identical. Further analyses showed the presence of 1 mol of phosphate/18500g of component Ml2 and less than 10% of this amount in component Ml3. Neither light component contained ribose. 4. Alkaline phosphatase from Escherichia coli converted component Ml2 into Ml3. Incubation with crude preparations of phosphorylase b kinase or protein kinase in the presence of ATP converted component Ml3 into Ml2. 5. Phosphorylation of component Ml3 with the kinases isolated from skeletal muscle and [γ-32P]ATP gave incorporation of 32P only into component Ml2 whether whole myosin or separated low-molecular-weight components were used. 6. High-voltage electrophoresis at pH6.5 and pH1.8 of a chymotryptic digest of 32P-labelled component Ml2 yielded one major radioactive peptide containing serine phosphate. 7. The amino acid sequence of this peptide was shown to be: Arg-Ala-Ala-Ala-Glu-Gly-Gly-(Ser,Ser(P))-Asn-Val-Phe. This sequence shows no obvious similarity to the site phosphorylated in the conversion of phosphorylase b into phosphorylase a by phosphorylase b kinase. 8. Evidence suggests that in vivo all the 18500-molecular-weight light chain is in the phosphorylated form. The extent of dephosphorylation that occurred during myosin extraction depended on the conditions employed.

scholarly journals The complete amino acid sequence of the low molecular weight cytosolic acid phosphatase

1989 ◽  
Vol 264 (5) ◽  
pp. 2560-2567
Author(s):  
G Camici ◽  
G Manao ◽  
G Cappugi ◽  
A Modesti ◽  
M Stefani ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Acid Phosphatase ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Low Molecular Weight ◽  
Complete Amino Acid Sequence

scholarly journals Characterization of Trypsin Inhibitor in Florunner Peanut Seeds (Arachis hypogaea L.)1

1988 ◽  
Vol 15 (2) ◽  
pp. 81-84 ◽  
Author(s):  
E. M. Ahmed ◽  
J. A. Applewhite
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Aspartic Acid ◽  
Arachis Hypogaea ◽  
Trypsin Inhibitor ◽  
Low Molecular Weight ◽  
Arachis Hypogaea L ◽  
Amino Acid Profiles ◽  
Low Levels

Abstract Florunner peanut seeds contained five trypsin isoinhibitors. Amino acid profiles of the trypsin inhibitors fraction showed high levels of aspartic acid, half-cystine and serine and low levels of histidine and tyrosine. The molecular weight of the inhibitor was 8.3 KDa. The presence of multiforms of this inhibitor, its low molecular weight and the high amount of half-cystine indicate that peanut trypsin inhibitor is of the Bowman-Birk type.

Normal Mature Human Enamel Protein

1979 ◽  
Vol 58 (2_suppl) ◽  
pp. 986-987 ◽  
Author(s):  
A. Belcourt
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Gel Electrophoresis ◽  
Protein Concentration ◽  
Polyacrylamide Gel Electrophoresis ◽  
Organic Matrix ◽  
Low Molecular Weight ◽  
Human Enamel ◽  
Weak Density ◽  
Enamel Protein

Pure enamel was prepared using an original microdissection technic. Protein concentration was 375 μg per gram of enamel. Polyacrylamide gel electrophoresis showed a single fast-migrating zone containing a thin double band. Ultracentrifugation studies suggested that the proteins were of low molecular weight or of weak density. Absorption spectra showed a strong absorbance at 260nm. Amino acid analyses yielded a composition of 25% Gly, 13.5% Glu, 11% Ser, 11% Pro, 2% Cys and 2% Hyp. A glucidic content of 15% was estimated and glucose, galactose, mannose and fucose were identified. The organic matrix of enamel seemed to be constituted of two major glycoproteins probably fibrous but different from keratin.

A Favorable, Narrow, δh Hansen-Parameter Domain for Gelation of Low-Molecular-Weight Amino Acid Derivatives

2011 ◽  
Vol 17 (48) ◽  
pp. 13603-13612 ◽  
Author(s):  
Pasquale Curcio ◽  
Florent Allix ◽  
Guillaume Pickaert ◽  
Brigitte Jamart-Grégoire
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Derivatives ◽  
Low Molecular Weight ◽  
Parameter Domain
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