Immobilization of pig muscle aldolase on a silica-based support

1989 ◽  
Vol 22 (3) ◽  
pp. 223-235 ◽  
Author(s):  
L. Horváth ◽  
Magdolna Ábrahám ◽  
L. Boross ◽  
B. Szajáni
Keyword(s):  
Pig Muscle ◽  
Pig Muscle Aldolase

Glyceraldehyde 3-Phosphate Dehydrogenase from Pig Muscle

Nature ◽  
1968 ◽  
Vol 219 (5158) ◽  
pp. 1025-1028 ◽  
Author(s):  
J. IEUAN HARRIS ◽  
RICHARD N. PERHAM
Keyword(s):  
Pig Muscle

scholarly journals Deciphering the microRNA transcriptome of skeletal muscle during porcine development

PeerJ ◽  
2016 ◽  
Vol 4 ◽  
pp. e1504 ◽  
Author(s):  
Miaomiao Mai ◽  
Long Jin ◽  
Shilin Tian ◽  
Rui Liu ◽  
Wenyao Huang ◽  
...  
Keyword(s):  
Muscle Development ◽  
Model Organism ◽  
Muscle Disease ◽  
Porcine Muscle ◽  
Development Stages ◽  
Age Related ◽  
Series Expression ◽  
Pig Muscle ◽  
Short Time

MicroRNAs (miRNAs) play critical roles in many important biological processes, such as growth and development in mammals. Various studies of porcine muscle development have mainly focused on identifying miRNAs that are important for fetal and adult muscle development; however, little is known about the role of miRNAs in middle-aged muscle development. Here, we present a comprehensive investigation of miRNA transcriptomes across five porcine muscle development stages, including one prenatal and four postnatal stages. We identified 404 known porcine miRNAs, 118 novel miRNAs, and 101 miRNAs that are conserved in other mammals. A set of universally abundant miRNAs was found across the distinct muscle development stages. This set of miRNAs may play important housekeeping roles that are involved in myogenesis. A short time-series expression miner analysis indicated significant variations in miRNA expression across distinct muscle development stages. We also found enhanced differentiation- and morphogenesis-related miRNA levels in the embryonic stage; conversely, apoptosis-related miRNA levels increased relatively later in muscle development. These results provide integral insight into miRNA function throughout pig muscle development stages. Our findings will promote further development of the pig as a model organism for human age-related muscle disease research.

Adenosine triphosphate concentration in guinea pig muscle after denervation

1957 ◽  
Vol 13 (3) ◽  
pp. 117-118 ◽  
Author(s):  
L. Michelazzi ◽  
M. A. Mor ◽  
M. U. Dianzani
Keyword(s):  
Guinea Pig ◽  
Adenosine Triphosphate ◽  
Pig Muscle

Differential recovery of acetylcholinesterase in guinea pig muscle and brain regions after soman treatment

1998 ◽  
Vol 17 (3) ◽  
pp. 157-162 ◽  
Author(s):  
Maxine C Lintern ◽  
Janet R Wetherell ◽  
Margaret E Smith
Keyword(s):  
Enzyme Activity ◽  
Time Course ◽  
Brain Regions ◽  
Similar Rate ◽  
Molecular Forms ◽  
Similar Degree ◽  
Brain Areas ◽  
Pig Muscle ◽  
Rate Of Recovery ◽  
The Brain

1 In brain areas of untreated guinea-pigs the highest activity of acetylcholinesterase was seen in the striatum and cerebellum, followed by the midbrain, medulla-pons and cortex, and the lowest in the hippocampus. The activity in diaphragm was sevenfold lower than in the hippocampus. 2 At 1 h after soman (27 mg/kg) administration the activity of the enzyme was dramatically reduced in all tissues studied. In muscle the three major molecular forms (A12, G4 and G1) showed a similar degree of inhibition and a similar rate of recovery and the activity had returned to normal by 7 days. 3 In the brain soman inhibited the G4 form more than the G1 form. The hippocampus, cortex and midbrain showed the greatest reductions in enzyme activity. At 7 days the activity in the cortex, medulla pons and striatum had recovered but in the hippocampus, midbrain and cerebellum it was still inhibited. 4 Thus the effects of soman administration varied in severity and time course in the different tissues studied. However the enzyme activity was still reduced in all tissues at 24 h when the overt signs of poisoning had disappeared.

Effect of dietary linoleic acid on the fatty acid composition of pig muscle

1990 ◽  
Vol 1990 ◽  
pp. 93-93
Author(s):  
M Enser ◽  
F M Whittington ◽  
J D Wood ◽  
D J Cole ◽  
J Wiseman
Keyword(s):  
Fatty Acid Composition ◽  
Fatty Acid ◽  
Linoleic Acid ◽  
Acid Composition ◽  
Neutral Lipids ◽  
Linoleic Acid Content ◽  
Pig Muscle ◽  
Species Specific ◽  
Feeding Diets ◽  
Cooked Meat

The fatty acid composition of meat has important effects on its succulence and flavour. The neutral lipids of muscle, are mainly energy stores resembling adipose tissue and affect the succulence of meat. However, the phospholipids, which are structural components of muscle, are important in the development of the species specific cooked meat flavour and odour. We have investigated the effects of feeding diets differing mainly in their linoleic acid content on the fatty acid composition of the lipids of M. Longissimus dorsi (LD) of pigs.

Caffeine stimulation of malignant hyperthermia-susceptible sarcoplasmic reticulum Ca2+ release channel

1994 ◽  
Vol 267 (5) ◽  
pp. C1253-C1261 ◽  
Author(s):  
N. H. Shomer ◽  
J. R. Mickelson ◽  
C. F. Louis
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Malignant Hyperthermia ◽  
Single Channel ◽  
Release Channel ◽  
Muscle Contracture ◽  
Malignant Hyperthermia Susceptible ◽  
Open Time ◽  
Pig Muscle ◽  
Channel Mutation ◽  
The Difference

The altered caffeine sensitivity of malignant hyperthermia-susceptible (MHS) muscle contracture is one basis of the diagnostic test for this syndrome. To determine whether the Arg615-to-Cys615 mutation of the porcine sarcoplasmic reticulum (SR) Ca2+ release channel is directly responsible for this altered caffeine sensitivity, the single-channel kinetics of purified MHS and normal pig Ca2+ release channels were examined. Initial studies demonstrated that decreasing the pH of the medium in either the cis- or trans-chamber decreased the Ca2+ release channel percent open time (Po). The half-inhibitory pH of MHS channels (6.86 +/- 0.04, n = 17) was significantly different from that of normal channels (7.08 +/- 0.07, n = 14). At pH 7.4, in either 7 or 0.12 microM Ca2+, MHS channel Po was not significantly different from that of normal channels over the range 0-10 mM caffeine. Although at pH 6.8 in 7 microM Ca2+ MHS channel Po was greater than that of normal channels over the range 0-20 mM caffeine, the difference could be eliminated by dividing each mean MHS Po by a scaling factor of 3.2. Thus the MHS Ca2+ release channel mutation does not appear to be directly responsible for the altered caffeine sensitivity of MHS pig muscle contracture. Rather, this altered caffeine sensitivity may result from an altered resting myoplasmic Ca2+ concentration or the altered pH and Ca2+ sensitivity of Ca2+ release channel Po of MHS muscle.

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