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Results for “PANCREATOPEPTIDASE”

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At least 19 recordsLinked to original sources
PubMed1995

The effect of pancreatopeptidase E (elastase) on anastomotic intimal thickness in two types of vascular prosthesis.

To determine the effects of pancreatopeptidase E (elastase) on anastomotic intimal thickness in vascular prostheses, expanded polytetrafluoroethylene (ePTFE) and Dacron grafts were implanted in the infrarenal aortas of 28 adult mongrel dogs, divided into four groups of seven dogs each according to the type of graft used and whether or not elastase was given. Thus, group E received ePTFE grafts without elastase; group D received Dacron grafts without elastase; group E + Ela received ePTFE grafts with concomitant oral elastase, 8 mg/kg per day; and group D + Ela received Dacron grafts with elastase given at the same dosage as in group E + Ela. Each graft was harvested 4 months following surgery for histologic examination. It was clearly observed that elastase suppressed intimal growth at the proximal and distal anastomoses in the ePTFE grafts (P < 0.05), but not in the Dacron grafts. Furthermore, when we measured the smooth muscle cell percent extinction (%E) on microspectrophotometry in the intima within 2 mm of the proximal and distal anastomoses, it was found that elastase reduced intimal smooth muscle proliferation at the anastomosis of the ePTFE grafts, but not the Dacron grafts (P < 0.05). These data suggest that elastase suppresses intimal growth by inhibiting smooth muscle cell migration and proliferation in the vascular prostheses of low but not of high porosity.

Anastomosis, Surgical↗
PubMedDate not supplied

Effect of pancreatopeptidase E (elastase) on the suppression of intimal fibrous proliferation after arterial reconstruction in high cholesterol fed rabbits.

The purpose of this study was to investigate the effect of pancreatopeptidase E (Elastase) administration on the healing of anastomosed arteries. A segment of infrarenal aorta was resected and reanastomosed in rabbits. In the control group, rabbits were fed commercial chow (ORC 4). In the cholesterol group, rabbits were fed a diet of 1% cholesterol added to ORC 4. In the Elastase group, rabbits were fed the same diet as the cholesterol group but received intraabdominal injections of Elastase. The rabbits were kept for 4 months and the abdominal aorta was retrieved for examination. All anastomosed aortas were patent. The cholesterol group developed aneurysmal dilatation in one and stenosis of the anastomosed sites due to hypergranulation in the remaining rabbits. Neither aneurysmal nor stenotic changes were detected in the other groups. We concluded that the administration of Elastase suppressed cholesterol induced atherosclerotic changes at the anastomotic sites in these animals.

Anastomosis, Surgical↗
PubMed1977

Chymotrypsinogen D, a new zymogen from porcine pancreas with proelastolytic activity.

During the purification of propancreatopeptidase E, a proATEEase activity is always copurified. The proelastolytic and proesterolytic activities can be separated on a hydroxylapatite column. The zymogen with potential ATEEase activity has a basic isoelectric point, can be activated by trypsin, and can hydrolyse elastin and ATEE but not ATAME. Its molecular weight is about 26,500 and the NH2-terminal sequence indicates clearly that it belongs to the chymotrypsinogen family, but that it is not chymotrypsinogen A, B, or C. We call it chymotrypsinogen D. Although both pancreatopeptidase E and chymotrypsin D can hydrolyse elastin, the synthetic substrate ATAME is attacked only by pancreatopeptidase E. Therefore, the peptide bonds in elastin cleaved by these two enzymes should be different.

Amino Acid Sequence↗
PubMed1975

The participation of methionine and cysteine in the formation of bonds resistant to the action of proteolytic enzymes in heated casein.

1. The influence of temperature, moisture content and the presence of glucose on the level of available methionine and cysteine in casein was studied. 2. Differences between total and available methionine and cysteine contents of heated casein (90 degrees for 24 h) were determined by an in vitro method. The maximum losses in total and available methionine content were 22 and 51% respectively. The losses in total and available cysteine content were 24 and 100% respectively. 3. The results indicated that for heated casein the release of amino acids by proteolytic enzymes was less complete than for native casein. 4. The results of rat growth assays suggested that diets containing oxidized casein are less well utilized by rats than those containing native casein. The decrease in body-weight of rats receiving the diets containing oxidized casein could be counteracted by the addition of methionine and 20 g unoxidized casein/kg diet. 5. There was a lower level of some available amino acids (determined after enzymic hydrolysis using pancreatopeptidase E (EC 3-4-4-7), leucine aminopeptidase (EC 3-4-I-I) and prolidase (EC 3-4-3-7)), including those essential for the rat, in oxidized casein as compared with native casein. 6. Cysteic acid, in oxidized casein, probably makes impossible the utilization of the amino acids in its neighbourhood. 7. From the differences in the available amino acid contents of the native, oxidized and heated casein it was concluded that the oxidation of casein causes the formation of complexes in the polypeptide chain, resistant to enzymic hydrolysis, but to a much lesser extent than does heating.

Amino Acids↗
PubMed1975

Electrophoretic characterization of porcine pancreatic (pro)elastases A and B.

Two porcine pancreatic zymogens can be separated by free electrophoresis on a sucrose gradient. After activation by trypsin, both enzymes can hydrolyze completely the fibrous protein elastin. One of the two proteins, proelastase B, has, in addition, an esterolytic activity towards N-acetyl-L-tyrosine ethyl ester. The other, proelastase A, does not possess it. The activation products of the zymogens have been tagged with radioactive diisopropylfluro-phosphonate and separated by polacrylamide-gel electrophoresis. Proelastase A gives only one active species, pancreatopeptidase E, but three distinct proteins can be obtained from proelastase B. Elastases A and B exhibit an important synergism when acting together upon a purified elastin lacking microfibrils. Trypsin has considerably less synergistic activity, and chymotrypsin has practically none.

Animals↗