scholarly journals Studies on the proteins of fish skeletal muscle. 6. Amino-acid composition of cod fibrillar proteins*

1959 ◽  
Vol 71 (1) ◽  
pp. 83-86 ◽  
Author(s):  
J. J. Connell ◽  
P. F. Howgate
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition

Effect of dietary restriction during gestation on amino acid composition and myofibrillar and collagen contents of skeletal muscle in gilts mated at puberty

1992 ◽  
Vol 40 (1) ◽  
pp. 98-106
Author(s):  
Constantinos G. Zarkadas ◽  
Elizabeth. Larmond ◽  
James I. Elliot ◽  
Ali D. Khalili ◽  
Carol. Beddard-Neil
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Dietary Restriction

scholarly journals Association of purified skeletal-muscle AMP deaminase with a histidine–proline-rich-glycoprotein-like molecule

1997 ◽  
Vol 326 (3) ◽  
pp. 641-648 ◽  
Author(s):  
Maria RANIERI-RAGGI ◽  
Umberto MONTALI ◽  
Francesca RONCA ◽  
Antonietta SABBATINI ◽  
Paul E. BROWN ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Rabbit Skeletal Muscle ◽  
Striking Similarity ◽  
The Novel ◽  
Amp Deaminase ◽  
Rabbit Plasma ◽  
N Terminus

Denaturation of rabbit skeletal-muscle AMP deaminase in acidic medium followed by chromatography on DEAE-cellulose in 8 M urea at pH 8.0 allows separation of two main peptide components of similar apparent molecular mass (75–80 kDa) that we tentatively assume correspond to two different enzyme subunits. Whereas the amino acid composition of one of the two peptides is in good agreement with that derived from the nucleotide sequence of the known rat and human AMPD1 cDNAs, the second component shows much higher contents of proline, glycine and histidine. N-Terminal sequence analysis of the fragments liberated by limited proteolysis with trypsin of the novel peptide reveals a striking similarity to the fragments produced by plasmin cleavage of the rabbit plasma protein called histidine–proline-rich glycoprotein (HPRG). However, some divergence is observed between the sequence of one of the fragments liberated from AMP deaminase by a more extensive trypsinization and rabbit plasma HPRG in the region containing residues 472–477. A fragment with a blocked N-terminus, which was found among those liberated by proteolysis with pepsin of either whole AMP deaminase or the novel component of the enzyme, shows an amino acid composition quite different from that of the N-terminus of the known subunit of AMP deaminase. By coupling this observation with the detection in freshly prepared AMP deaminase of a low yield of the sequence (LTPTDX) corresponding to that of HPRG N-terminus, it can be deduced that in comparison with HPRG, the putative HPRG-like component of AMP deaminase contains an additional fragment with a blocked N-terminus, which is liberated by a proteolytic process during purification of the enzyme. The implications of the association to rabbit skeletal-muscle AMP deaminase of a HPRG-like protein species are discussed.

Molecular weight and amino acid composition of five-times-crystallized phosphoglucose isomerase from rabbit skeletal muscle

Biochemistry ◽  
1970 ◽  
Vol 9 (7) ◽  
pp. 1506-1514 ◽  
Author(s):  
Ning G. Pon ◽  
Klaus D. Schnackerz ◽  
Michael N. Blackburn ◽  
Gora C. Chatterjee ◽  
Ernst A. Noltmann
Keyword(s):  
Skeletal Muscle ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Phosphoglucose Isomerase ◽  
Rabbit Skeletal Muscle

M-line protein preparations from frog skeletal muscle: isolation and localization of an M-line protein and a 105 000 dalton polypeptide contaminant

1980 ◽  
Vol 58 (6) ◽  
pp. 516-526 ◽  
Author(s):  
Z. C. Dhanarajan ◽  
Burr G. Atkinson
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Cross Reactivity ◽  
Frog Muscle ◽  
Rabbit Muscle ◽  
Frog Skeletal Muscle ◽  
Protein Preparation ◽  
Chicken Muscle

A 165 000 dalton polypeptide was purified and characterized from high salt extracted crude M-line protein preparations of frog skeletal muscle. It has an isoelectric point of 5.8–6.2 and an amino acid composition similar to that reported for the putative M-line protein in chicken muscle (termed component I) and rabbit muscle. Antibodies prepared against the 165 000 dalton polypeptide do not react with purified frog debranching enzyme, and indirect immunofluorescent studies localize this polypeptide wholly in the middle of the A band (presumably the M line) of frog skeletal muscle. We conclude that this 165 000 dalton polypeptide is a basic constituent of the M line in frog skeletal muscle.Crude M-line protein preparations from frog muscle invariably contained a 105 000 dalton polypeptide contaminant. In crude M-line protein preparation from chicken muscle, a polypeptide with a similar molecular mass was identified as phosphorylase b. Characterization of the 105 000 dalton polypeptide isolated from crude M-line protein preparations establishes that in frog muscle extracts this component has an amino acid composition which is different from phosphorylase b, but similar to frog α-actinin. Since it also exhibits immunochemical cross-reactivity with α-actinin and not with purified phosphorylase b, and is localized wholly at the Z line, we conclude that the 105 000 dalton polypeptide contaminant in crude M-line protein preparations from frog muscle is α-actinin.

scholarly journals Affinity-chromatographic isolation and some properties of troponin C from different muscle types

1977 ◽  
Vol 161 (3) ◽  
pp. 465-471 ◽  
Author(s):  
J F Head ◽  
R A Weeks ◽  
S V Perry
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Troponin I ◽  
Smooth Muscles ◽  
Troponin C ◽  
Electrophoretic Mobilities ◽  
Muscle Types ◽  
Chromatographic Isolation

1. The formation of a complex between troponin I and troponin C that is stable in 6M-urea and dependent on Ca2+ was demonstrated in extracts of vertebrate striated and smooth muscles. 2. A method using troponin I coupled to Sepharose is described for the rapid isolation of troponin C from striated and smooth muscles of vertebrates. 3. Troponin C of rabbit cardiac muscle differs significantly in amino acid composition from troponin C of skeletal muscle. The primary structures of troponin C of red and white skeletal muscle are very similar. 4. The troponin C-like protein isolated from rabbit uterus muscle has a slightly different amino acid composition, but possess many similar properties to the forms of troponin C isolated from other muscle types. 5. The electrophoretic mobilities of the I-troponin C complexes formed from components isolated from different muscle types are determined by the troponin I component.

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