COMPARATIVE STUDY OF AUTOLYTIC CHANGES  IN PORK AND BEEF MUSCLE TISSUE PROTEOME

The paper presents the studies on the autolytic transformations in pork and beef samples by proteomic methods. The changes in the protein fractions were analyzed by one-dimensional and two- dimensional electrophoresis with the following identification by mass-spectrometric methods. The changes in muscle proteins in the course of autolytic processes were found. For example, the intensity of the protein spots of pyruvate kinase, myosin light chains and adenylate kinase increased during autolysis. The fragments of myosin light chains appeared. The activity of the endogenous enzymes, such as calpain 3 and cathepsin D in the course autolysis was also studied. During the first 24 hours after animal slaughter, the activity of these enzymes reached the maximum level and then decreased. The results of the performed investigations confirmed that pork and beef have different rate of autolysis but similar proteomic changes.

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Muscle protein analysis. II. Two-dimensional electrophoresis of normal and diseased human skeletal muscle.

Clinical Chemistry ◽

10.1093/clinchem/26.8.1152 ◽

1980 ◽

Vol 26 (8) ◽

pp. 1152-1155 ◽

Cited By ~ 37

Author(s):

C S Giometti ◽

M Bárány ◽

M J Danon ◽

N G Anderson

Keyword(s):

Muscle Protein ◽

Human Muscle ◽

Light Chains ◽

Myosin Light Chains ◽

Two Dimensional ◽

Normal Muscle ◽

Two Dimensional Electrophoresis ◽

Three Samples ◽

Normal Human ◽

Dimensional Electrophoresis

Abstract We used high-resolution two-dimensional electrophoresis to analyze the major proteins of normal and pathological human-muscle samples. The normal human-muscle pattern contains four myosin light chains: three that co-migrate with the myosin light chains from rabbit fast muscle (extensor digitorum longus), and one that co-migrates with the light chain 2 from rabbit slow muscle (soleus). Of seven Duchenne muscular dystrophy samples, four yielded patterns with decreased amounts of actin and myosin relative to normal muscle, while three samples gave patterns comparable to that for normal muscle. Six samples from patients with myotonic dystrophy also gave normal patterns. In nemaline rod myopathy, in contrast, the pattern was deficient in two of the fast-type myosin light chains.

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Bacterial proteomics and its application for pathogenesis studies

Current Pharmaceutical Biotechnology ◽

10.2174/1389201022666210908153234 ◽

2021 ◽

Vol 22 ◽

Author(s):

Mahdi Asghari Ozma ◽

Ehsaneh Khodadadi ◽

Mohammad Ahangarzadeh Rezaee ◽

Mohammad Asgharzadeh ◽

Mohammad Aghazadeh ◽

...

Keyword(s):

Biofilm Formation ◽

Essential Role ◽

Bacterial Pathogenesis ◽

Accurate Diagnosis ◽

Post Translational Modifications ◽

Two Dimensional Electrophoresis ◽

Bacterial Proteins ◽

Comprehensive Information ◽

Dimensional Electrophoresis ◽

Proteomic Methods

: Bacteria build their structures by implementing several macromolecules such as proteins, polysaccharides, phospholipids, and nucleic acids, which leads to preserve their lives and play an essential role in their pathogenesis. There are two genomic and proteomic methods to study various macromolecules of bacteria, which are complementary methods and provide comprehensive information. Proteomic approaches are used to identify proteins and their cell applications. Furthermore, to study bacterial proteins, macromolecules are involved in the bacteria's structures and functions. These protein-based methods provide comprehensive information about the cells, such as the external structures, internal compositions, post-translational modifications, and mechanisms of particular actions such as biofilm formation, antibiotic resistance, and adaptation to the environment, which are helpful in promoting bacterial pathogenesis. These methods use various devices such as MALDI-TOF MS, LC-MS, and two-dimensional electrophoresis, which are valuable tools for studying different structural and functional proteins of the bacteria and their mechanisms of pathogenesis that causes rapid, easy, and accurate diagnosis of the infections.

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Two-dimensional electrophoresis of heart muscle proteins in human cardiomyopathies

Electrophoresis ◽

10.1002/elps.1150110412 ◽

1990 ◽

Vol 11 (4) ◽

pp. 333-336 ◽

Cited By ~ 12

Author(s):

Leonid I. Kovalyov ◽

Vladimir G. Naumov ◽

Helena V. Pulyayeva ◽

Anatoli M. Samko ◽

Marina N. Tsvetkova ◽

...

Keyword(s):

Heart Muscle ◽

Two Dimensional ◽

Muscle Proteins ◽

Two Dimensional Electrophoresis ◽

Dimensional Electrophoresis

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Optimization of Two-Dimensional Electrophoresis Condition for Rice Grain Protein and Comparison of Relevant Proteomic Methods

ACTA AGRONOMICA SINICA ◽

10.3724/sp.j.1006.2012.00921 ◽

2013 ◽

Vol 38 (5) ◽

pp. 921-927

Author(s):

Qi-Song LI ◽

Jun CHEN ◽

Shi-Sheng LIN ◽

Zhong LI ◽

Zhi-Xing ZHANG ◽

...

Keyword(s):

Grain Protein ◽

Rice Grain ◽

Two Dimensional ◽

Two Dimensional Electrophoresis ◽

Dimensional Electrophoresis ◽

Proteomic Methods

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GENIC VARIATION IN ABUNDANT SOLUBLE PROTEINS OF DROSOPHILA MELANOGASTER AND DROSOPHILA PSEUDOOBSCURA

Genetics ◽

10.1093/genetics/102.3.437 ◽

1982 ◽

Vol 102 (3) ◽

pp. 437-453

Author(s):

Rama S Singh ◽

Michael B Coulthart

Keyword(s):

Drosophila Melanogaster ◽

Gel Electrophoresis ◽

Polyacrylamide Gel Electrophoresis ◽

Soluble Proteins ◽

One Dimensional ◽

Two Dimensional Electrophoresis ◽

Genic Variation ◽

Soluble Enzymes ◽

Coomassie Brilliant ◽

Dimensional Electrophoresis

ABSTRACT Genic variation was surveyed for 20 proteins of Drosophila melanogaster and 18 proteins of D. pseudoobscura. Analysis was by extraction and one-dimensional polyacrylamide gel electrophoresis under nondenaturing conditions, followed by staining with Coomassie Brilliant Blue to detect soluble proteins present in relatively large amounts ("abundant soluble proteins"). D. melanogaster was polymorphic for 65% of its protein loci and an individual was heterozygous for 10% of its loci. The respective figures for D. pseudoobscura were 61% and 11%. These estimates of genic variation fall between previously published estimates obtained for these species by one-dimensional electrophoresis of soluble enzymes and those obtained by two-dimensional electrophoresis of solubilized abundant proteins. However, variation for both species could be strongly partitioned between loci, on the basis of tissue and stage expression of the proteins. The results are discussed with respect to their bearing on the possibility that abundant proteins constitute a distinct class of proteins less polymorphic than soluble enzymes.

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Comparative study of weaning pigs' muscle proteins using two-dimensional electrophoresis

Potravinarstvo Slovak Journal of Food Sciences ◽

10.5219/1449 ◽

2021 ◽

Vol 15 ◽

pp. 52-57

Author(s):

Anastasia Akhremko ◽

Liliya Fedulova

Keyword(s):

Protein Modification ◽

Protein Identification ◽

Muscle Protein ◽

Growth Period ◽

Farm Animals ◽

Phosphoglycerate Mutase ◽

Two Dimensional ◽

Muscle Proteins ◽

Two Dimensional Electrophoresis ◽

Dimensional Electrophoresis

The proteostasis system of animals, including various types of protein modification during the growth stage, leads to an almost incomprehensible number of possible forms of protein, and each can regulate numerous functions. In the presented work, the composition of muscle tissue protein from different portions of piglets was studied to understand the main muscle protein formation. Comparative analysis of weaned piglets' main muscle protein from l. dorsi, biceps femoris, and brachiocephalicus were analyzed using two-dimensional electrophoresis. Changes in the staining intensity of protein fractions inherent in different muscles were revealed. As part of this work, candidate groups of pig muscle proteins have been selected. Eleven protein spots were revealed for the longest muscle of the back, and seven for the biceps; the muscles of the neck are characterized by indicators of low protein fraction volume. Among the proteins found, myosin light chains, phosphoglycerate mutase, troponins, and adenylate kinase is most likely present. The obtained results of protein identification in muscle tissues, obtained during the intensive growth period, will allow a more detailed understanding of protein regulation, function, and interactions in complex biological systems, which will subsequently be significantly important for biomonitoring health and predicting farm animals productivity.

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GENETIC VARIATION IN PROTEINS: COMPARISON OF ONE-DIMENSIONAL AND TWO-DIMENSIONAL GEL ELECTROPHORESIS

Genetics ◽

10.1093/genetics/104.2.381 ◽

1983 ◽

Vol 104 (2) ◽

pp. 381-390

Author(s):

Tracy McLellan ◽

Giovanna Ferro-Luzzi Ames ◽

Kishiko Nikaido

Keyword(s):

Genetic Variation ◽

Two Dimensional ◽

Two Dimensional Gel Electrophoresis ◽

One Dimensional ◽

Two Dimensional Electrophoresis ◽

Related Proteins ◽

Dimensional Electrophoresis ◽

Denaturation Of Proteins ◽

New Mutations ◽

Limited Sensitivity

ABSTRACT Two proteins with known characteristics on one-dimensional gels were studied by two-dimensional electrophoresis to compare the sensitivities of the two methods in detecting genetic variation. Two-dimensional electrophoresis was found to be less sensitive than several types of one-dimensional gels in distinguishing variants of both proteins. Denaturation of proteins in urea in the two-dimensional method makes it possible to distinguish closely related proteins that differ from each other by units of charge. Many more types of variation in protein sequences can be distinguished on one-dimensional gels in the absence of denaturants. The estimates of heterozygosity based on two-dimensional gels are lower than those based on other methods, at least in part, because of the limited types of sequence differences that can be detected on two-dimensional gels. The application of two-dimensional electrophoresis to the measurement of genetic variation and to the detection of new mutations should be made carefully, in view of the limited sensitivity of the method in finding differences in sequence.

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Characterization of human muscle myosins with respect to the light chains

Biochemical Journal ◽

10.1042/bj1950251 ◽

1981 ◽

Vol 195 (1) ◽

pp. 251-258 ◽

Cited By ~ 25

Author(s):

P Volpe ◽

D Biral ◽

E Damiani ◽

A Margreth

Keyword(s):

Light Chain ◽

Mammalian Species ◽

Cross Reactivity ◽

Light Chains ◽

Two Dimensional Electrophoresis ◽

Fast Myosin ◽

Chain Composition ◽

Fast Light ◽

Dimensional Electrophoresis

Isolated myosins from human predominantly fast and slow muscles, human neonatal and foetal muscle were examined for light chain composition by one- and two-dimensional electrophoresis. The LC1F, LC2F and LC3F light chains were identical with their counterparts from rabbit fast myosin. Human LC1S was identified by correlative criteria as a single component having a molecular weight slightly lower than, but an electric charge similar to, that of rabbit LC1Sb. Consequently, human LC1S appears to be much less heterogeneous relative to LC1F than is the case with other mammalian species. A high immunological cross-reactivity was likewise observed, with antibody specific to rabbit LC1F, between the isolated myosins from several human mixed muscles and rabbit fast myosin, though reactivity was highest with foetal myosin (having a pure-fast-light-chain pattern).

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