Potent debriding ability of collagenolytic protease isolated from the hepatopancreas of the king crab Paralithodes camtschatica

1993 ◽  
Vol 285 (1-2) ◽  
pp. 32-35 ◽  
Author(s):  
I. Y. Sakharov ◽  
S. P. Glyanzev ◽  
F. E. Litvin ◽  
T. V. Savvina
Keyword(s):  
King Crab ◽  
Collagenolytic Protease ◽  
Paralithodes Camtschatica

scholarly journals STUDIES ON PROTEOLYTIC ENZYME OF LIVER OF KING CRAB, PARALITHODES CAMTSCHATICA (TILESIUS)-I

1962 ◽  
Vol 28 (10) ◽  
pp. 1015-1019 ◽  
Author(s):  
Tsuneyuki SAITO ◽  
Yoshio ISHIHARA ◽  
Yoshiaki MAITA ◽  
Yasuzo ITO
Keyword(s):  
Proteolytic Enzyme ◽  
King Crab ◽  
Paralithodes Camtschatica

Purification and some properties of elastase from hepatopancreas of king crab Paralithodes camtschatica

1993 ◽  
Vol 106 (3) ◽  
pp. 681-684 ◽  
Author(s):  
Ivan Yu. Sakharov ◽  
Alexandra V. Dzunkovskaya ◽  
Alexandr A. Artyukov ◽  
Nataliya N. Zakharova
Keyword(s):  
King Crab ◽  
Paralithodes Camtschatica

Infestation by Brood Symbionts and Their Impact on Egg Mortality of the Red King Crab, Paralithodes camtschatica, in Alaska: Geographic and Temporal Variation

1991 ◽  
Vol 48 (4) ◽  
pp. 559-568 ◽  
Author(s):  
Armand M. Kuris ◽  
S. Forrest Blau ◽  
A. J. Paul ◽  
Jeffrey D. Shields ◽  
Daniel E. Wickham
Keyword(s):  
Life History ◽  
Life Cycle ◽  
Temporal Variation ◽  
Seasonal Pattern ◽  
Red King Crab ◽  
King Crab ◽  
Egg Masses ◽  
Egg Mortality ◽  
Paralithodes Camtschatica

Egg masses of 772 red king crab, Paralithodes camtschatica, were sampled to determine the prevalence, intensity, and patterns of cooccurrence of brood symbionts from 28 Alaskan localities. Carcinonemertes regicides and three other undescribed nemertean egg predators were recovered from many localities, as were an undescribed turbellarian and an amphipod, Ischyrocerus sp. A widespread outbreak of nemerteans occurred in the 1983–84 and 1984–85 red king crab brooding seasons. At some locations, nearly all of the eggs were consumed in the 1983–84 brood season. Feeding of C. regicides on eggs was documented in vitro and these worms caused substantial egg mortality at many locations. The amphipod was also an egg predator and may have had a significant impact at three locations. The turbellarian did not kill eggs. From the seasonal pattern of C. regicides infestation at Kachemak Bay, we postulate an abbreviated life cycle and autoinfection for C. regicides. Such life history features may have contributed to the peak intensities observed late in the 1983–84 and 1984–85 brooding seasons. At some localities, heavy brood mortality may reduce or eliminate recruitment of some year classes to the fishery.

Substrate specificity of collagenolytic proteases from the king crab Paralithodes camtschatica

1994 ◽  
Vol 107 (3) ◽  
pp. 411-417 ◽  
Author(s):  
Ivan Yu. Sakharov ◽  
Fedor E. Litvin ◽  
Olga V. Mitkevitch ◽  
Gennady P. Samokhin ◽  
Zhanna D. Bespalova
Keyword(s):  
Substrate Specificity ◽  
King Crab ◽  
Collagenolytic Proteases ◽  
Paralithodes Camtschatica

scholarly journals Temperature and the regulation of enzyme activity in poikilotherms. Regulatory properties of fructose diphosphatase from muscle of the Alaskan king-crab

1971 ◽  
Vol 121 (3) ◽  
pp. 399-409 ◽  
Author(s):  
Hans W. Behrisch
Keyword(s):  
Skeletal Muscle ◽  
Enzyme Activity ◽  
Low Temperature ◽  
Temperature Sensitive ◽  
King Crab ◽  
Rate Limiting Step ◽  
Low Concentrations ◽  
Higher Temperature ◽  
Paralithodes Camtschatica ◽  
Rate Limiting

1. The properties of fructose diphosphatase from skeletal muscle of the Alaskan king-crab (Paralithodes camtschatica) were examined over the physiological temperature range of the animal. 2. King-crab muscle fructose diphosphatase is first activated by Na+ and NH4+ and is then partially inhibited by these cations at concentrations higher than 10mm at 0°, 8° and 15°C. Enzyme activity is stimulated by K+ at 0°C, but is curtailed at 8°C and 15°C, an effect that could render rate independent of temperature. 3. Affinity for substrate increases with decreasing temperature; below the temperature of acclimatization, Km for fructose 1,6-diphosphate increases, resulting in a complex U-shaped temperature–Km curve. 4. King-crab muscle fructose diphosphatase is inhibited by low concentrations of AMP. As with enzymes of other poikilotherms, inhibition by AMP is sensitive to temperature; the enzyme is least sensitive to inhibition by AMP near the temperature of acclimatization. 5. The affinity of fructose diphosphatase for fructose 1,6-diphosphate is enhanced by phosphoenolpyruvate, and this activation is temperature-sensitive; 0.5mm-phosphoenolpyruvate causes a sevenfold decrease in Km for fructose 1,6-diphosphate at 15°C but a 25-fold decrease at 0°C. 6. Phosphoenolpyruvate appears to decrease the affinity of king-crab muscle fructose diphosphatase for AMP at low temperature, whereas at the higher temperature it appears to enhance inhibition by AMP. Phosphoenolpyruvate was not observed to cause a reversal of inhibition of fructose diphosphatase activity by AMP. The identification of phosphoenolpyruvate as an activator of a rate-limiting step in gluconeogenesis permits the suggestion of a coupling of the controlling mechanisms of several steps in the glycolytic and gluconeogenic chains. 7. These findings suggest mechanisms for the maintenance and regulation of control of fructose diphosphatase activity in king-crab skeletal muscle at low temperature and under conditions that favour concomitant activity of phosphofructokinase.

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