scholarly journals A comparative analysis of bone and cartilage metabolism in two strains of guinea-pig with varying degrees of naturally occurring osteoarthritis

2002 ◽  
Vol 10 (10) ◽  
pp. 758-767 ◽  
Author(s):  
J.L. Huebner ◽  
M.A. Hanes ◽  
B. Beekman ◽  
J.M. TeKoppele ◽  
V.B. Kraus
Keyword(s):  
Comparative Analysis ◽  
Guinea Pig ◽  
Cartilage Metabolism ◽  
Naturally Occurring ◽  
And Cartilage

scholarly journals Hydrolysis of a naturally occurring β-glucoside by a broad-specificity β-glucosidase from liver

1986 ◽  
Vol 237 (2) ◽  
pp. 469-476 ◽  
Author(s):  
K L LaMarco ◽  
R H Glew
Keyword(s):  
Guinea Pig ◽  
Competitive Inhibitor ◽  
Heat Denaturation ◽  
Pig Liver ◽  
Naturally Occurring ◽  
Aryl Glycosides ◽  
Beta Glucosidase ◽  
Hydrolysis Of ◽  
Guinea Pig Liver ◽  
Broad Specificity

We have isolated from guinea-pig liver a broad-specificity beta-glucosidase of unknown function that utilizes as its substrate non-physiological aryl glycosides (e.g. 4-methylumbelliferyl beta-D-glucopyranoside, p-nitrophenyl beta-D-glucopyranoside). The present paper documents that this enzyme can be inhibited by various naturally occurring glycosides, including L-picein, dhurrin and glucocheirolin. In addition, L-picein, which acts as a competitive inhibitor of the broad-specificity beta-glucosidase (Ki 0.65 mM), is also a substrate for this enzyme (Km 0.63 mM; Vmax. 277,000 units/mg). Heat-denaturation, kinetic competition studies, chromatographic properties and pH optima all argue strongly that the broad-specificity beta-glucosidase is responsible for the hydrolysis of both the non-physiological aryl glycosides and L-picein. This paper demonstrates that beta-glucosidase can catalyse the hydrolysis of a natural glycoside, and may provide a key to understanding the function of this enigmatic enzyme. A possible role in the metabolism of xenobiotic compounds is discussed.

Diurnal Variation in the Response of the Mandible to Orthopedic Force

2002 ◽  
Vol 81 (10) ◽  
pp. 711-715 ◽  
Author(s):  
S. Yamada ◽  
S. Saeki ◽  
I. Takahashi ◽  
K. Igarashi ◽  
H. Shinoda ◽  
...  
Keyword(s):  
Diurnal Variation ◽  
Dark Period ◽  
Time Of Day ◽  
Light Period ◽  
Considerable Reduction ◽  
Cartilage Metabolism ◽  
Differentiation And Proliferation ◽  
And Cartilage

Bone and cartilage metabolism is known to be more active during rest than during periods of activity. The purpose of this study was to examine the hypothesis that mandibular retractive force could be more effective when applied to rats during rest. Mandibular retractive force caused a considerable reduction in the condylar length in experimental groups, and the magnitude of this reduction was greater in the Light-period (08:00-20:00) group than in the Dark-period (20:00-08:00) group. The differentiation and proliferation of chondrocytes were inhibited in animals in the Light-period group, compared with those in the Dark-period group. These results suggest that the orthopedic effects of mandibular retractive force vary depending on the time of day the force is applied, and that such force may be more effective while animals are resting than while they are active.

scholarly journals Humanized NOG mice as a model for tuberculosis vaccine-induced immunity: a comparative analysis with the mouse and guinea pig models of tuberculosis

Immunology ◽  
2017 ◽  
Vol 152 (1) ◽  
pp. 150-162 ◽  
Author(s):  
Ajay Grover ◽  
Amber Troy ◽  
Jenny Rowe ◽  
JoLynn M. Troudt ◽  
Elizabeth Creissen ◽  
...  
Keyword(s):  
Comparative Analysis ◽  
Guinea Pig ◽  
Nog Mice ◽  
Induced Immunity

scholarly journals 84 HOW DOES VITAMIN D AFFECT BONE AND CARTILAGE IN THE SPONTANEOUS GUINEA PIG MODEL OF OSTEOARTHRITIS?

2007 ◽  
Vol 15 ◽  
pp. C57
Author(s):  
T.A. Hunt ◽  
R. Kandel ◽  
R. Renlund ◽  
R. Vieth ◽  
M. Grynpas
Keyword(s):  
Vitamin D ◽  
Guinea Pig ◽  
Pig Model ◽  
Guinea Pig Model ◽  
And Cartilage

Characterization of zymosan-induced arthritis in the rat: Effects on joint inflammation and cartilage metabolism

Life Sciences ◽  
1994 ◽  
Vol 55 (17) ◽  
pp. PL321-PL326 ◽  
Author(s):  
P. Gegout ◽  
P. Gillet ◽  
D. Chevrier ◽  
C. Guingamp ◽  
B. Terlain ◽  
...  
Keyword(s):  
Joint Inflammation ◽  
Cartilage Metabolism ◽  
And Cartilage

scholarly journals Naturally Occurring Parelaphostrongylus tenuis–Associated Choriomeningitis in a Guinea Pig With Neurologic Signs

2012 ◽  
Vol 50 (3) ◽  
pp. 560-562 ◽  
Author(s):  
T. Southard ◽  
H. Bender ◽  
S. E. Wade ◽  
C. Grunenwald ◽  
R. W. Gerhold
Keyword(s):  
Guinea Pig ◽  
Naturally Occurring ◽  
Parelaphostrongylus Tenuis

scholarly journals THE OCCURRENCE AND DISTRIBUTION OF ATROPINESTERASE, AND THE SPECIFICITY OF TROPINESTERASES

1941 ◽  
Vol 25 (2) ◽  
pp. 197-205 ◽  
Author(s):  
David Glick ◽  
Susi Glaubach
Keyword(s):  
Guinea Pig ◽  
Egg White ◽  
Pig Liver ◽  
Naturally Occurring ◽  
Hydrolysis Of ◽  
Guinea Pig Liver

Atropinesterase was found to exist in approximately one out of every four rabbits, and no relation could be observed between the incidence of the enzyme and season, sex, color, age, or weight. The occurrence of the enzyme was also shown to be unrelated to that of cholinesterase. The distribution of atropinesterase in the blood and organs of rabbits was studied; the animals devoid of the enzyme in their blood contained no demonstrable activity in any of the organ extracts tested. The presence of atropinesterase in frog liver, and its absence from the serum, has been confirmed. Hydrolysis of homatropine, but not atropine, by guinea pig liver was observed, while the serum was without action on either of the compounds. On this basis the possibility arises that guinea pig liver contains a homatropinesterase enzyme separate from atropinesterase. It was shown that lack of atropinesterase activity in certain rabbits is not likely to be due to the presence of a naturally occurring inhibitor. It has been demonstrated that contrary to previous indications neither fresh egg white nor yolk possess atropinesterase activity. The specificity of tropinesterases was investigated and evidence was presented for the possible existence of two distinct enzymes, cocainesterase and tropacocainesterase.

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