Proteomic analysis of mdx skeletal muscle: Great reduction of adenylate kinase 1 expression and enzymatic activity

PROTEOMICS ◽  
2003 ◽  
Vol 3 (10) ◽  
pp. 1895-1903 ◽  
Author(s):  
Yue Ge ◽  
Mark P. Molloy ◽  
Jeffrey S. Chamberlain ◽  
Philip C. Andrews
Keyword(s):  
Skeletal Muscle ◽  
Enzymatic Activity ◽  
Great Reduction ◽  
Adenylate Kinase ◽  
Proteomic Analysis ◽  
Adenylate Kinase 1

Immunization with recombinant schistosome adenylate kinase 1 partially protects mice against Schistosoma japonicum infection

2017 ◽  
Vol 116 (6) ◽  
pp. 1665-1674 ◽  
Author(s):  
Yanru Gao ◽  
Xiaoshan Zhou ◽  
Huan Wang ◽  
Rong Liu ◽  
Qing Ye ◽  
...  
Keyword(s):  
Schistosoma Japonicum ◽  
Adenylate Kinase ◽  
Adenylate Kinase 1

scholarly journals Proteomic analysis of secreted proteins from skeletal muscle cells during differentiation

2014 ◽  
Vol 5 ◽  
pp. 1-9 ◽  
Author(s):  
Koichi Ojima ◽  
Mika Oe ◽  
Ikuyo Nakajima ◽  
Masahiro Shibata ◽  
Koichi Chikuni ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Proteomic Analysis ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Secreted Proteins

Proteomic analysis reveals changes in energy metabolism of skeletal muscle in beef cattle supplemented with vitamin A

2020 ◽  
Vol 100 (8) ◽  
pp. 3536-3543 ◽  
Author(s):  
Carolina F Campos ◽  
Thaís C Costa ◽  
Rafael T S Rodrigues ◽  
Simone E F Guimarães ◽  
Felipe H Moura ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Energy Metabolism ◽  
Vitamin A ◽  
Beef Cattle ◽  
Proteomic Analysis

Immunoinhibition and automated column chromatography compared for assay of creatine kinase isoenzyme MB in serum.

1982 ◽  
Vol 28 (1) ◽  
pp. 166-169 ◽  
Author(s):  
P M Bayer ◽  
M Boehm ◽  
P Hajdusich ◽  
H Hotschek ◽  
H Koehn ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
Skeletal Muscle ◽  
Adenylate Kinase ◽  
Kinase Activity ◽  
High Ratio ◽  
Creatine Kinase Isoenzyme ◽  
Fourth Group ◽  
The Third ◽  
Altered Surface ◽  
Creatine Kinase Isoenzyme Mb

Abstract We examined sera from six different groups of patients for CK-MB activity by means of two commercially available tests, an immunoinhibition method (E. Merck) and the CK-MB test as used with the aca (Du Pont). In the first group of patients (suspicion of myocardial infarction) the correlation between the two methods was good: r = 0.9191, y = 1.068x -- 0.888, x = 18.7 U/L, y = 19.0 U/L. In the second group, patients with high adenylate kinase activity, no interference was detectable on the aca, whereas the immunoinhibition method yielded falsely high CK-MB values. The third group consisted of persons with macro-CK-BB in their serum. In the immunoinhibition test these patients usually showed a high CK-MB:total CK ratio, whereas such results were rarely found for the aca. The fourth group, patients with a different electrophoretic mobility of their CK-isoenzymes (migration of an active band towards the cathode), were detected by the immunoinhibition method (high ratio of CK-MB to total CK), but not with the aca. In the presence of free CK-BB (group five) the immunoinhibition test resulted in "falsely" high CK-MB values, whereas CK-BB was retained on the column of the aca. In skeletal muscle diseases (group six) results by the two methods differed, values for CK-MB on the aca being much higher. It was demonstrated experimentally that this was due to CK-MM with altered surface charge.

Unusual Variant of Lactate Dehydrogenase Isoenzymes

1975 ◽  
Vol 21 (1) ◽  
pp. 162-164 ◽  
Author(s):  
D H Buchholz ◽  
R K Donabedian
Keyword(s):  
Skeletal Muscle ◽  
Lymph Node ◽  
Lactate Dehydrogenase ◽  
Enzymatic Activity ◽  
Genetic Locus ◽  
Negro Woman ◽  
Unusual Variant ◽  
Heterozygous Form ◽  
Monomeric Proteins ◽  
Lactate Dehydrogenase Isoenzymes

Abstract Thirteen electrophoretic bands of lactate dehydrogenase isoenzyme activity were detected in the serum of a 69-year-old Negro woman who died of pseudomonas pneumonia. No evidence of tumor was found at necropsy, and additional studies of the enzymatic activity of crude extracts of liver, lung, spleen, kidney, brain, skeletal muscle, lymph node, and heart revealed 1, 2, 3, 4, and 5 separate isoenzyme bands for lactate dehydrogenase isoenzymes 1, 2, 3, 4, and 5, respectively (a total of 15 isoenzyme bands). Serum and erythrocyte hemolysate from one of two healthy daughters displayed a similar pattern of multiple isoenzyme bands in isoenzymes 2 and 3. The observed pattern is consistent with the heterozygous form of a mutation of the genetic locus controlling synthesis of the M monomer such that two differently charged monomeric proteins are produced, each of which apparently combines with H chains with equal facility, leading to the multiband enzymatic specificity seen.

Sign in / Sign up

Export Citation Format

Share Document