Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.22.6 (chymopapain)
 407 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A spinal cord injury model is described using chymopapain as a neurotoxic agent in rats. The trauma was evaluated by neurophysiological and morphological methods. Electrically evoked compound action potentials were used to quantify the neurophysiological effects caused by the injection of chymopapain into the lumbar dural theca in rats. A branch of the sciatic nerve was stimulated with voltage impulses of constant amplitude (40 V) and duration (0.1 ms) at the right external malleolus. The responses were recorded at the dorsal root entry zone L1. We used different doses of the enzyme (1000 i.u./ml; 2500 i.u./ml; 5000 i.u./ml). A total amount of 0.1 ml was injected into the rats' lumbar spinal canal intrathecally (n = 18). The control rate (n = 8) were subjected to exactly the same stimulus and recording procedures but the test solution was a corresponding volume of isotonic saline. Two hours after injection the animals were examined clinically and then sacrificed for histology. The prolongation of the latency of the electrically evoked potentials caused by the enzyme was very clear at the doses of 2500 i.u. and 5000 i.u. being about 10-15% relative to the mean latency before administration of the drug. The histological evaluation showed hemorrhage, vascular damage and indirect signs of myelin edema of the lumbar nerve tissue. Our study indicates that chymopapain injections into the lumbar spinal canal can be used as a reproducible model for spinal cord injury research.
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PMID:Intrathecal injection of a specific enzyme in rats as a model for chemically induced spinal cord injury. 207 8

Chymopapain (EC 3.4.22.6) was purified from commercially available dried latex of papaya (Carica papaya) by extraction at acidic pH, cation-exchange chromatography and active site-directed affinity chromatography on immobilized alanyl-phenyl-alaninaldehyde semicarbazone, with elution by mercuric chloride. The product was found by immunoassay to be essentially free of the other cysteine proteinases from papaya, including papaya proteinase IV, and was fully active. The rate of alkylation of the active site cysteine of chymopapain by iodoacetate was found to be sufficiently rapid and selective for this reagent to be used as an active-site titrant.
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PMID:The preparation of fully active chymopapain free of contaminating proteinases. 208 14

Chymopapain is a polypeptide of 218 amino acid residues. It has considerable structural similarity with papain and papaya proteinase omega, including conservation of the catalytic site and of the disulphide bonding. Chymopapain is like papaya proteinase omega in carrying four extra residues between papain positions 168 and 169, but differs from both papaya proteinases in the composition of its S2 subsite, as well as in having a second thiol group, Cys-117. Some evidence for the amino acid sequence of chymopapain has been deposited as Supplementary Publication SUP 50153 (12 pages) at the British Library Document Supply Centre, Boston Spa., Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained on the terms indicated in Biochem. J. (1990) 265, 5. The information comprises Supplement Tables 1-4, which contain, in order, amino acid compositions of peptides from tryptic, peptic, CNBr and mild acid cleavages, Supplement Fig. 1, showing re-fractionation of selected peaks from Fig. 2 of the main paper. Supplement Fig. 2, showing cation-exchange chromatography of the earliest-eluted peak of Fig. 3 of the main paper, Supplement Fig. 3, showing reverse-phase h.p.l.c. of the later-eluted peak from Fig. 3 of the main paper, and Supplement Fig. 4, showing the separation of peptides after mild acid hydrolysis of CNBr-cleavage fragment CB3.
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PMID:The amino acid sequence of chymopapain from Carica papaya. 210 78

The allergic response to chymopapain intradiscal therapy has been well documented. The most serious of these reactions is anaphylactic shock, which may result in death. Various screening methods, including skin tests, have been proposed to identify susceptible patients. Anaphylactic shock occurred in a 40-year-old woman from application of the screening skin test. Appropriate therapeutic intervention should be readily accessible when this test is performed.
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PMID:Anaphylactic shock associated with chymopapain skin test. A case report and review of the literature. 222 22

The effect of externally applied spinal loads on facet mechanics before and after facet capsulectomy and disc alteration was investigated. Four control and four chymopapain-treated specimens were tested. Facet load and resultant load location were determined in the unaltered state, after facet capsulectomy, and after discectomy using a newly developed, noninvasive measurement technique. Resultant contact load locations shifted in a predictable manner. Caudal shift in contact locations occurred with chymopapain treatment or discectomy but was variable with capsulectomy. Facet load changed with applied load magnitude and direction; no significant change was noted after intradiscal chymopapain, discectomy, or capsulectomy. The significance of the lack of force change with disc narrowing is unknown. Perhaps, observed facet degeneration results from a change in the joint motion and contact location rather than change in facet load.
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PMID:Facet loads in the canine lumbar spine before and after disc alteration. 225 91

We carried out a randomized comparison study with 69 patients, one group of whom had been operated on (41) and the other group treated by chemonucleolysis with chymopapain (25) in order to arrive at an objective picture of the latter recently much criticised method. 88% of the patients who were treated with chymopapain showed lasting success, and almost 90% of the operated patients are also in a good condition. In our opinion, complications can be avoided and the patient can be spared a surgical operation by the correct choice of patients and proper performance of the method in standby anaesthesia. This justifies the performance of chemonucleolysis with chymopapain.
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PMID:[Chemonucleolysis with chymopapain in lumbar disk hernia. Randomized comparative study with operated patients]. 226 6

This study is based on 20 patients who underwent bone scanning before and after chemonucleolysis (CN) for a herniated lumbar disk. It shows that chymopapain, the proteolytic enzyme used for CN, does not induce early or late bone lesions of the adjacent vertebral plates. Abnormal uptake by one of the vertebral plates indicates a "chemical discitis." The pattern observed on the bone scan is different from the one presented by patients with bacterial spondylitis.
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PMID:Bone scan and chemonucleolysis. 227 34

Because arachnoiditis occurred in a previous experimental study, the authors performed additional experimental injections of chymopapain in the epidural space. Four monkeys received epidural injections of 100 units of chymopapain in 1.2 mL of saline on days 1, 8, and 16 of the experiment; four control animals received injections of 1.2 mL of 0.9% saline on the same days. Both groups were killed on the 84th day. The dural sac was removed, fixed, sectioned, stained, and examined microscopically. No significant changes were found in the arachnoid, dura, or epidural space of the treated animals. Chymopapain, even if injected repeatedly into the epidural space, does not cause significant scarring in the meninges.
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PMID:Effect of repeated injections of chymopapain in the epidural space. 229 52

The author's experience in the use of chymopapain for the lysis of ruptured disc indicates that the drug is a valuable alternative to surgery.
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PMID:An update on chymopapain for treating lumbar disc ruptures. 231 72

Chemonucleolysis has recently become an established treatment for intervertebral disc protrusion. However, the exact mechanism of chemonucleolysis is still unknown. If mechanisms of chemonucleolysis include diminution of intradiscal pressure followed by subsequent regeneration of the nucleus pulposus, then a more selective enzyme for glycosaminoglycan, chondroitinase ABC, might be used for chemonucleolysis instead of chymopapain. Thus experimental chemonucleolysis with chondroitinase ABC compared with chymopapain was investigated. In rabbits, chondroitinase ABC is as effective for chemonucleolysis as chymopapain, but the chemonucleolysis process with chondroitinase ABC was milder than with chymopapain. At an early chemonucleolysis phase, chondroitinase ABC action was chiefly limited to digestion of the matrix, and a large number of cells in the nucleus pulposus remained. During long-term observations of chemonucleolysis with chondroitinase ABC, nuclear structure was restored to a nearly normal state. Although limited, this study indicates that chondroitinase ABC might be more suitable than chymopapain for chemonucleolysis.
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PMID:Experimental chemonucleolysis with chondroitinase ABC. 231 86


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