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.

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 Homology between a histidine-rich protein from Plasmodium lophurae and a protein associated with the knob-like protrusions on membranes of erythrocytes infected with Plasmodium falciparum.

1980 ◽  
Vol 151 (6) ◽  
pp. 1534-1538 ◽  
Author(s):  
A Kilejian
Keyword(s):  
Amino Acids ◽  
Plasmodium Falciparum ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Immunoelectron Microscopy ◽  
Protein Hydrolysate ◽  
Cross Reactivity ◽  
Plasmodium Lophurae

The incorporation of several radioactive amino acids into the knob protein of Plasmodium falciparum was compared. Histidine showed better incorporation than proline. A protein hydrolysate, which had all major amino acids except histidine and methionine, showed relatively poor incorporation as compared with proline, and no labeling could be detected with methionine or leucine. These results strongly suggest that the amino acid composition of the knob protein has the same peculiarities as that of a histidine-rich protein characterized from P. lophurae. Immunoelectron microscopy suggested possible immunological cross-reactivity between these two proteins.

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

scholarly journals The random character of protein evolution and its effects on the reliability of phylogenetic information deduced from amino acid sequences and compositions

1980 ◽  
Vol 191 (2) ◽  
pp. 349-354 ◽  
Author(s):  
A Cornish-Bowden
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Random Effect ◽  
Cross Reactivity ◽  
Amino Acid Sequences ◽  
Random Errors ◽  
Phylogenetic Information ◽  
Rates Of Evolution ◽  
Related Pair

Because evolution occurs by random events, the actual number of substitutions that occur in any period is not exactly equal to the number expected from the mean rate of substitution, but is statistically distributed about it. In consequence, even if rates of evolution are constant in different lineages, ‘trees’ deduced from descendant protein sequences contain random errors. When there are fewer than about eight differences between the sequences of the most distantly related pair from a set of proteins, this random effect is very large. It can then render trivial the statistical disadvantage inherent in using a crude measure of protein difference, such as amino acid composition or immunological cross-reactivity, in preference to a measure based the sequences of the most distantly related pair from a set of proteins, this random effect is very large. It can then render trivial the statistical disadvantage inherent in using a crude measure of protein difference, such as amino acid composition or immunological cross-reactivity, in preference to a measure based the sequences of the most distantly related pair from a set of proteins, this random effect is very large. It can then render trivial the statistical disadvantage inherent in using a crude measure of protein difference, such as amino acid composition or immunological cross-reactivity, in preference to a measure based on amino acid sequence. In some cases, such as classification of mammals on the basis of cytochrome c structure, it appears to make little difference to the reliability of the results whether the sequences of the protein concerned are known or not. It may also be possible to obtain more reliable phylogenetic information from composition measurements on several kinds of protein than one could obtain from sequence measurements on a single kind of protein.

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