The effects of potassium and muscle homogenate on proprioceptive responses in crayfish and crab

2017 ◽  
Vol 327 (6) ◽  
pp. 366-379 ◽  
Author(s):  
Cole Malloy ◽  
Viresh Dayaram ◽  
Sarah Martha ◽  
Brenda Alvarez ◽  
Ikenna Chukwudolue ◽  
...  
Keyword(s):  
Muscle Homogenate

Electron Beam-Induced Mass Loss in Freeze-Dried Tissue and Protein Samples

1985 ◽  
Vol 43 ◽  
pp. 470-471
Author(s):  
M.E. Cantino ◽  
M.K. Goddard ◽  
L.E. Wilkinson ◽  
D.E. Johnson
Keyword(s):  
Electron Beam ◽  
Salivary Gland ◽  
Mass Loss ◽  
Counting Rate ◽  
Dose Dependence ◽  
X Ray ◽  
Large Samples ◽  
Freeze Dried ◽  
Muscle Homogenate ◽  
Large Muscle

Quantification in biological x-ray microanalysis depends on accurate evaluation of mass loss. Although several studies have addressed the problem of electron beam induced mass loss from organic samples (eg., 1,2). uncertainty persists as to the dose dependence, the extent of loss, the elemental constituents affected, and the variation in loss for different materials and tissues. in the work described here, we used x-ray counting rate changes to measure mass loss in albumin (used as a quantification standard), salivary gland, and muscle.In order to measure mass loss at low doses (10-4 coul/cm2 ) large samples were needed. While freeze-dried salivary gland sections of the required dimensions were available, muscle sections of this size were difficult to obtain. To simulate large muscle sections, frog or rat muscle homogenate was injected between formvar films which were then stretched over slot grids and freeze-dried. Albumin samples were prepared by a similar procedure. using a solution of bovine serum albumin in water. Samples were irradiated in the STEM mode of a JEOL 100C.

Dissolution of Fish Muscle Homogenates by Lysolecithin

1968 ◽  
Vol 25 (10) ◽  
pp. 2157-2164
Author(s):  
R. E. E. Jonas
Keyword(s):  
Skeletal Muscle ◽  
Rainbow Trout ◽  
Snake Venom ◽  
Incubation Medium ◽  
Fish Muscle ◽  
N Content ◽  
Snake Venom Phospholipase ◽  
Solubilizing Activity ◽  
Supernatant Solution ◽  
Muscle Homogenate

On incubating skeletal muscle homogenates from rainbow trout with lysolecithin (LL) and comparing them with homogenates of the same muscle without added LL, and after centrifuging the mixtures, it was found that the N content of the supernatant solution of the homogenate containing LL was about 20% higher than that of the homogenate without LL. Increases close to maximum in N content of the supernatant solution were found to occur at a concentration of about 4 mg LL per ml of incubation medium containing 100 mg muscle in 3.0 ml of 0.9% NaCl at a pH of 6.0–8.0 and at about 35 C for a period of 1 hr. Snake venom phospholipase A added to muscle homogenate showed no solubilizing activity and α-tocopherol acetate and cortisol showed irregular stimulation. It was concluded that LL exerts a solubilizing action on fish muscle homogenates.

THE RELEASE OF BOUND CORTICOSTEROIDS FROM THE MUSCLE OF THE TOAD (XENOPUS LAEVIS)

1967 ◽  
Vol 37 (2) ◽  
pp. 221-225 ◽  
Author(s):  
D. BELLAMY ◽  
J. G. PHILLIPS ◽  
RUTH A. LEONARD
Keyword(s):  
Xenopus Laevis ◽  
Small Particle ◽  
Subcellular Fraction ◽  
Circulatory System ◽  
Fresh Medium ◽  
Particulate Fraction ◽  
Particle Fraction ◽  
Limb Muscles ◽  
Copper Zinc ◽  
Muscle Homogenate

SUMMARY After the injection of cortisol into the toad Xenopus laevis, the concentration of steroid in the main circulatory system was much higher than that in the limb muscles. The concentration of corticosteroids in the blood fell at a faster rate than that in muscle. The particulate fraction of toad muscle homogenate bound added cortisol and some of it was not removed by repeated washing of the tissue with fresh medium. Bound steroid was not confined to any one subcellular fraction. The small particle fraction ('microsomes') contained the greatest proportion of steroid and the highest steroid concentration. The loss of corticosteroids from intact and washed particle preparations of toad gastrocnemius was not influenced by temperature over the range of 17–37°. Copper, zinc and manganese (between 26 and 31 mm) inhibited the release of cortisol bound to muscle particles; p-chloromercuribenzoate (2 mm) and anoxia had no effect. A variation in pH from 2 to 10 made little difference to the rate of steroid release by muscle particles suspended in 0·15 m-KC1. The results suggest that the release of strongly bound steroids from muscle does not involve an enzymic mechanism.

STUDIES ON THE TRANSAMINASE ACTIVITY OF MUSCLE TISSUE FROM ALLATECTOMIZED ROACHES, PERIPLANETA AMERICANA

1960 ◽  
Vol 38 (2) ◽  
pp. 275-283 ◽  
Author(s):  
Shu-Yi Wang ◽  
S. E. Dixon
Keyword(s):  
Muscle Tissue ◽  
Spectrophotometric Method ◽  
Periplaneta Americana ◽  
Transaminase Activity ◽  
Oxalacetic Acid ◽  
Significant Difference ◽  
The Difference ◽  
Muscle Homogenate

The transaminase activity of roach muscle homogenate was measured by the spectrophotometric method for oxalacetic acid. The transaminase activity of muscle from allatectomized roaches of both sexes of adults and nymphs was significantly lower than in normal animals. There was also a significant difference between sexes. The reduction in transaminase activity of muscle from female adults was about twice that of male adults but between nymphs the difference due to sex was not nearly so striking. The activity of muscle tissue due to allatectomy was considerably more reduced in male nymphs than in male adults. The significance of these results is discussed.

scholarly journals THE SARCOTUBULAR SYSTEM OF FROG SKELETAL MUSCLE

1961 ◽  
Vol 10 (4) ◽  
pp. 201-218 ◽  
Author(s):  
U. Muscatello ◽  
Ebba Andersson-Cedergren ◽  
G. F. Azzone ◽  
Alexandra von der Decken
Keyword(s):  
Skeletal Muscle ◽  
Skeletal Muscle Cell ◽  
Mitochondrial Atpase ◽  
Frog Skeletal Muscle ◽  
Structural Components ◽  
Mitochondrial Fragmentation ◽  
Mitochondrial Membranes ◽  
Sarcotubular System ◽  
Relaxing Effect ◽  
Muscle Homogenate

In the frog skeletal muscle cell a well defined and highly organized system of tubular elements is located in the sarcoplasm between the myofibrils. The sarcoplasmic component is called the sarcotubular system. By means of differential centrifugation it has been possible to isolate from the frog muscle homogenate a fraction composed of small vesicles, tubules, and particles. This fraction is without cytochrome oxidase activity, which is localized in the mitochondrial membranes. This indicates that the structural components of this fraction do not derive from the mitochondrial fragmentation, but probably from the sarcotubular system. This fraction, called sarcotubular fraction, has a Mg++-stimulated ATPase activity which differs from that of muscle mitochondria in that it is 3 to 4 times higher on the protein basis as compared with the mitochondrial ATPase, and is inhibited by Ca++ and by deoxycholate like the Kielley and Meyerhof ATPase. We therefore conclude that the "granules" of the Kielley and Meyerhof ATPase, which were shown to have a relaxing effect, are fragments of the sarcotubular system. The isolated sarcotubular fraction has a high RNA content and demonstrable activity in incorporating labeled amino acids, even in the absence of added supernatant.

scholarly journals Carbonic anhydrase C in white-skeletal-muscle tissue

1982 ◽  
Vol 205 (3) ◽  
pp. 559-566 ◽  
Author(s):  
W Siffert ◽  
G Gros
Keyword(s):  
Skeletal Muscle ◽  
Carbonic Anhydrase ◽  
Skeletal Muscles ◽  
Michaelis Constant ◽  
Turnover Number ◽  
Muscle Enzyme ◽  
Flow Apparatus ◽  
Type C ◽  
Erythrocyte Carbonic Anhydrase ◽  
Muscle Homogenate

We investigated the activity of carbonic anhydrase in blood-free perfused white skeletal muscles of the rabbit. Carbonic anhydrase activities were measured in supernatants and in Triton extracts of the particulate fractions of white-skeletal-muscle homogenate by using a rapid-reaction stopped-flow apparatus equipped with a pH electrode. An average carbonic anhydrase concentration of about 0.5 microM was determined for white skeletal muscle. This concentration is about 1% of that inside the erythrocyte. Some 85% of the muscle enzyme was found in the homogenate supernatant, and only 15% appeared to be associated with membranes and organelles. White-skeletal-muscle carbonic anhydrase was characterized in terms of its Michaelis constant and catalytic-centre activity (turnover number) for CO2 and its inhibition constant towards ethoxzolamide. These properties were identical with those of the rabbit erythrocyte carbonic anhydrase C, suggesting that a type-C enzyme is present in white skeletal muscle. Affinity chromatography of muscle supernatant and of lysed erythrocytes showed that, whereas rabbit erythrocytes contain about equal amounts of carbonic anhydrase isoenzymes B and C, the B isoenzyme is practically absent from white skeletal muscle. Similarly, ethoxzolamide-inhibition curves suggested that white skeletal muscle contains no carbonic anhydrase A. It is concluded that white skeletal muscle contains essentially one carbonic anhydrase isoenzyme, the C form, most of which is probably of cytosolic origin.

Preparation of heavy meromyosin from the autolyzed squid mantle muscle homogenate

2005 ◽  
Vol 71 (1) ◽  
pp. 213-219 ◽  
Author(s):  
Takeya YOSHIOKA ◽  
Yasunori KINOSHITA ◽  
Sanae KATO ◽  
Young-Je CHO ◽  
Kunihiko KONNO
Keyword(s):  
Heavy Meromyosin ◽  
Muscle Homogenate

Studies on Adenylate Cyclase – Cyclic AMP System of the Myopathic Hamster (UM-X7.1) Skeletal and Cardiac Muscles

1975 ◽  
Vol 53 (10) ◽  
pp. 1122-1127 ◽  
Author(s):  
J. A. C. Harrow ◽  
J. N. Singh ◽  
G. Jasmin ◽  
N. S. Dhalla
Keyword(s):  
Skeletal Muscle ◽  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Skeletal Muscles ◽  
Normal Values ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Amp System ◽  
Cardiac Muscles ◽  
Muscle Homogenate

Cyclic AMP content, adenylate cyclase (EC 4.6.1.1) activity and phosphodiesterase I (EC 3.1.4.1) activity of the hind leg skeletal muscle and cardiac muscle in 60- and 150-day-old normal and myopathic (UM-X7.1) hamsters were examined. In 60-day-old myopathic animals, cardiac cyclic AMP levels were higher and phosphodiesterase I activity was lower, without any changes in the basal adenylate cyclase activity, whereas in 150-day-old myopathic hamsters, cardiac cyclic AMP and basal adenylate cyclase activity were lower, without any changes in the homogenate phosphodiesterase I activity. On the other hand, basal adenylate cyclase and phosphodiesterase I activities in the skeletal muscle homogenate from 60- and 150-day-old myopathic animals were not different from the normal values but the skeletal muscle cyclic AMP levels were significantly less in 60-day-old myopathic hamsters only. The plasma cyclic AMP levels in 60-day-old myopathic hamsters, unlike 150-day-old myopathic animals, were higher than the normal. Although these results reveal differences in myopathic cardiac and skeletal muscles, it is concluded that changes in adenylate cyclase – cyclic AMP system in myopathy are dependent upon the degree of disease.

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