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1.
OBJECTIVE: To purify canine carbonic anhydrase isoenzyme III (CA-III) and determine plasma, serum, and tissue concentrations of CA-III in healthy dogs and dogs with experimentally induced muscle damage. ANIMALS: 121 healthy Beagles. PROCEDURE: Muscle was obtained from 2 Beagles after euthanasia, and CA-III was purified and characterized by use of column chromatography and electrophoresis, respectively. A CA-III-specific ELISA was developed to determine concentrations of CA-III in plasma of 116 dogs and tissues of 1 dog. Serum creatine kinase (CK) activity and CA-III concentration were also determined before and after induction of muscle damage by IM injection of 2 ml of 10% lidocaine to 2 dogs. RESULTS: Canine CA-III had a molecular weight of 28 kd and an isoelectric point of 8.2. Mean (+/- SD) concentration of CA-III in plasma of healthy dogs was 16.91 +/- 9.55 ng/ml. The highest tissue concentration of CA-III was detected in skeletal muscle. Serum concentration of CA-III increased and peaked within the first 2 to 3 hours after induction of muscle damage. The increase in CA-III concentration was more rapid than that of CK activity, and concentration reached its maximum and returned to baseline sooner than did CK activity. CONCLUSIONS AND CLINICAL RELEVANCE: The CA-III ELISA we developed was a sensitive method for determining CA-III concentrations in plasma, serum samples, and tissue specimens of dogs. Use of this ELISA requires only a small volume of serum and may enable the study of changes in CA isoenzyme concentrations associated with muscle disorders in dogs. 相似文献
2.
Heat-induced structural changes and aggregation properties of walleye pollack myosin, light meromyosin (LMM) and heavy meromyosin (HMM) were investigated. According to the circular dichroism (CD) measurement, the α-helix content of the pollack myosin and LMM were estimated to be 72% and 90% at 5°C but decreased to 22% and 21% by increasing the temperature to 60°C with two transitions at 35°C and 50°C, respectively. In contrast, that of HMM decreased gradually from 37% to 33% by increasing the temperature from 5°C to 40°C, and decreased steeply to 20% above 50°C. These results indicate that the decrease in the α-helix content in the myosin molecule upon heating was attributable mainly to the decrease in the α-helix content in the LMM region. In contrast, 1-anilinonaphthalene-8-sulfonate (ANS) fluorescence and light scattering intensity of both myosin and HMM were remarkably increased above 25°C and 35°C, respectively, while those of LMM showed only a slight change even above 60°C. Although LMM alone formed no aggregates detectable by the light scattering measurement, it formed coprecipitates with myosin but not with HMM upon heating at 40°C for 10 min. These facts suggest that LMM bind to the LMM region of the myosin. Further, it was found that myosin gel formed in a test tube by the same heating conditions was significantly weakened by coexistence of LMM. These results suggest that the association of the LMM region of myosin molecules is essential for the heat-induced gelation of myosin. 相似文献
3.
Toshiho Nishita Daisuke Yorifuji Kensuke Orito Nobutsune Ichihara Kazuyoshi Arishima 《Acta veterinaria Scandinavica》2012,54(1):34
Background
The levels and immunohistochemical localization of muscle carbonic anhydrase III (CA-III) in healthy chickens and in muscular dystrophia affected (DA) chickens show that the muscles of diseased animal undergo a progressive increase of enzyme activity.Methods
An enzyme-linked immunoassay was used to assess the CA-III levels in the muscles and other tissues from eight normal White Leghorn chickens and in two chickens with muscular dystrophy. Immunohistochemical localization of the enzyme in the muscles of these animals was also determined.Results
The levels of CA-III in the tensor fasciae latae and the superficial pectoral muscles of the DA chickens were higher than the level in normal chickens. The concentrations of CA-III in erythrocytes and plasma from diseased chickens were approximately 15-fold and 1.4-fold higher than in the normal chickens, respectively. In the superficial pectoral and the tensor fasciae latae muscles of diseased chickens, the numbers of strongly stained and weakly stained fibers were greater than that in the normal chickens.Conclusion
The levels of CA-III in the superficial pectoral muscle, the tensor fasciae latae muscle, plasma and erythrocytes from the chickens with muscular dystrophy were higher than found in normal chickens. 相似文献4.
Nishita T Takahasi M Kasuya T Matsui K Ichihara N Murakami M Asari M 《The Journal of veterinary medical science / the Japanese Society of Veterinary Science》2005,67(1):63-67
Equine carbonic anhydrase isozymes (CA-I and CA-II) were purified from erythrocytes by several column chromatography. Polyclonal anti-CA-I and anti-CA-II sera were produced in rabbits. Sensitive competitive enzyme-linked immunosorbent assays (ELISA) were established to determine the developmental changes in CA-I and CA-II levels in equine erythrocytes. Concentrations of CA-I and CA-II in erythrocytes from 150 clinically normal thoroughbreds (123 racehorses and 27 riding horses) were determined by ELISA. Mean (+/- SD) concentrations of CA-I and CA-II in racehorses were 1.70 +/- 0.48 and 0.94 +/- 0.13 mg/g hemoglobin (Hb), respectively. Mean concentrations of CA-I and CA-II in riding horses were 2.34 +/- 0.52 and 0.76 +/- 0.08 mg/g Hb, respectively. When the CA levels in racehorses and riding horses were compared, the CA-I level in riding horses was higher than that in racehorses (p=0.01). The CA-II level in racehorses was higher than that in riding horses (p=0.02). These data suggest that the levels of CA isozymes in erythrocytes of racehorses were influenced by chronic physical stress. The CA-I concentration in erythrocytes of 2-month-old horses was approximately 0.25 mg/g Hb. The CA-I level noticeably increased during the first year of life and approached normal adult levels by 2 years. The CA-II level decreased slightly with age, indicating different regulation of CA-I and CA-II expression during development. 相似文献
5.
Kaseda M Ichihara N Nishita T Amasaki H Asari M 《The Journal of veterinary medical science / the Japanese Society of Veterinary Science》2006,68(2):131-135
In the present study, we firstly demonstrated immunohistochemical expressions of secretory carbonic anhydrase (CA-VI) isozyme in bovine forestomach, large intestine and major salivary glands. CA-VI was detected in basal layer epithelial cells of esophageal and forestomach stratified epithelium, in mucous cells of upper glandular region of large intestine, in serous acinar cells of the parotid gland, in serous demilune cells and some ductal liner cells of mandibular, monostomatic sublingual and esophageal glands. These immunohistolocalizations suggested that bovine CA-VI plays various roles in pH regulation, maintenance of ion and fluid balance, and cell proliferation. 相似文献
6.
Toshiho NISHITA Ryou ANEZAKI Kazunori MATSUNAGA Kensuke ORITO Tamae KASUYA Hideyo SAKANOUE Akiko MATSUNAGA Kazuyoshi ARISHIMA 《Journal of Equine Science》2013,24(4):57-62
Although endoscopy is the definitive diagnostic method for the detection of colonic
ulcers, the equipment required for performing the test is costly and difficult to use.
Therefore, a simple cost-effective and reliable screening test for intestinal tract
bleeding is needed. To this end, we measured carbonic anhydrase isozymes (CA-I and CA-II)
originating from erythrocytes by ELISA in order to determine if they could be used as
markers of occult blood in feces. For fecal extract preparation, 2 g of feces were mixed
with 4 ml of 0.01 M Tris-HCl (pH 8.0) containing 0.01% thimerosal. The concentrations of
CA-I and CA-II in the fecal samples of 13 clinically normal racehorses were found to be
30.0 ± 10.0 and 34.0 ± 13.0 ng/ml, respectively. Increased concentrations of CA-I were
detected in the fecal samples of 5 horses after blood administration; however, no increase
was observed in CA-II. The concentrations of CA-I and CA-II in the fecal samples of 88
racehorses with clinical signs of equine gastric ulcer syndrome (EGUS) were 115.3 ± 79.0
and 41.0 ± 42.0 ng/ml, respectively. Thus, our results indicate that CA isozymes can be
useful as markers of occult blood in the fecal samples of horses with intestinal tract
bleeding. 相似文献
7.
Ichihara N Ishikawa T Kaseda M Nishita T Amasaki H Asari M 《The Journal of veterinary medical science / the Japanese Society of Veterinary Science》2006,68(12):1363-1365
The immunolocalization of the efferent duct and the epididymis in canine was firstly examined using an the immunohistochemical method with the canine carbonic anhydrase (CA) -I, CA-II and CA-III antisera. The efferent duct was immunonegative for all present canine CA antisera. However, some slender shaped epithelial cells in the head and body segments of the epididymal duct were intensely reacted to the CA-II antiserum. These results suggested that the CA-II might be controlled in the luminal environment in the head and body segments of the canine epididymis by the proton and bicarbonate balance for the maintenance of the spermatozoal stability and movement. 相似文献
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Toshiho Nishita Yuichiro Tomita Takao Imanari Nobutsune Ichihara Kensuke Orito Kazuyoshi Arishima 《Acta veterinaria Scandinavica》2011,53(1):16