ABSTRACT
Optimal conditions are determined for isolation and purification of peroxidase (EC 1.11.1.7) from the mixed human saliva by gel-filtration and ion chromatography. Such properties as pH and temperature optima, molecular weight, Km, amino acid composition, the effect of activators and inhibitors (purified saliva peroxidases and commercial preparation of horse-radish peroxidase "Reanal", Hungary) are studied with the use of different substrates. The data obtained are necessary to optimize production processes of isolation, storage and methods of the experimental and clinical application of peroxidases of different origin.
Subject(s)
Peroxidases/metabolism , Saliva/enzymology , Amino Acids/analysis , Catalysis , Chromatography, Gel , Horseradish Peroxidase/metabolism , Humans , Hydrogen-Ion Concentration , Molecular Weight , TemperatureABSTRACT
Proteinase inhibitor activity in patients with stage IIb, III and IV breast cancer was shown to be higher than in healthy donors and cases with stage I-IIa disease. The proteinase activity/inhibitor activity ratio in breast carcinoma tissue appeared higher than in benign tumors and normal tissue. Tumor proteinase activity was in reverse correlation with degree of cell differentiation. Dissemination to regional lymph nodes involved decrease in tumor proteinase activity matched by relevant increase in lymph nodes. Radiation treatment resulted in decreased proteinase activity and increased inhibitory activity both in primary tumor and involved lymph nodes.
Subject(s)
Breast Neoplasms/enzymology , Endopeptidases/blood , Breast Neoplasms/pathology , Breast Neoplasms/radiotherapy , Female , Humans , Hydrolysis , Lymphatic Metastasis , Neoplasm Staging , Protease Inhibitors/bloodABSTRACT
Intramuscular administration of trypsin and kallikrein (andecaline) into rats contributed to more favourable development of acute traumatic pancreatitis. Trypsin and andecaline prevented the activation of proteinases in blood serum and pancreas and promoted an increase in content of trypsin inhibitor in blood serum. The proteinases efficiency appears to depend on elevation of general resistance of the organism to the trauma.
Subject(s)
Kallikreins/therapeutic use , Pancreatitis/enzymology , Peptide Hydrolases/blood , Protease Inhibitors/blood , Trypsin/therapeutic use , Acute Disease , Animals , Enzyme Activation , Hydrolysis , Pancreatitis/drug therapy , Rats , Rats, Inbred StrainsSubject(s)
Blood , Peptide Hydrolases/blood , Peritonitis/blood , Animals , Biological Transport , Rats , Rats, Inbred StrainsSubject(s)
Peptide Hydrolases/metabolism , Peritoneum/metabolism , Peritonitis/drug therapy , Protease Inhibitors/therapeutic use , Toxemia/etiology , Absorption , Animals , Female , Humans , Male , Peptide Hydrolases/blood , Peritonitis/complications , Peritonitis/enzymology , Rats , Rats, Inbred StrainsSubject(s)
Aldosterone/pharmacology , Hydrocortisone/pharmacology , Kallikreins/pharmacology , Parotid Gland/enzymology , Submandibular Gland/enzymology , Animals , Carboxylic Ester Hydrolases/metabolism , Deoxyribonucleases/metabolism , Drug Interactions , Male , Rats , Rats, Inbred Strains , Ribonucleases/metabolism , alpha-Amylases/metabolismSubject(s)
Neoplasms/enzymology , Peptide Hydrolases/metabolism , Protease Inhibitors/therapeutic use , Animals , Aprotinin/therapeutic use , Breast Neoplasms/enzymology , Cathepsin B , Cathepsins/metabolism , Cell Transformation, Neoplastic , Female , Humans , Laryngeal Neoplasms/enzymology , Lung Neoplasms/enzymology , Mice , Neoplasms/drug therapy , Ovarian Neoplasms/enzymology , Pancreatic Neoplasms/enzymology , Pepstatins/therapeutic use , Rats , Stomach Neoplasms/enzymology , alpha 1-Antitrypsin/metabolismSubject(s)
Kallikreins/physiology , Kinins/physiology , Stomach/physiology , Animals , Bradykinin/administration & dosage , Bradykinin/pharmacology , Cell Division/drug effects , Diuresis/drug effects , Dogs , Drug Interactions , Gastric Mucosa/metabolism , Gastrointestinal Motility/drug effects , Glucocorticoids/physiology , Kallikreins/pharmacology , Mineralocorticoids/physiology , Prostaglandins/physiology , Renin-Angiotensin System , Vasopressins/administration & dosageABSTRACT
Proteolytic activity was studied in human saliva, gingiva and in other tissues of oral cavity by means of hydrolysis of N-alpha-benzoyl-L-arginine ethyl ester (BAEE), protamine and hemoglobin. Alkaline proteinases were mainly observed in gingiva, leukocytes and in a precipitate of mixed saliva. Acid proteinases (pH 3.5) were localized in submaxillary saliva. In a liquid fraction of saliva maximal proteolytic activity was estimated both at pH 3.5 (by hydrolysis of hemoglobin), at pH 8.0 (hydrolysis of BAEE and protamine) and at pH 9.3 (only in experiments with protamine). The protamine-splitting activity at pH 9.3 was found only in parotid saliva. The optima of the proteolytic enzymes activity were at pH 3.5 (substrate hemoglobin) and at pH 7.5 (substrates protamine and BAEE) in precipitate of mixed saliva and in gingiva. Effects of several inhibitors, chelating agents, thiol-containing substances and metal ions on the proteolytic activity in saliva were studied.
Subject(s)
Gingiva/enzymology , Peptide Hydrolases/metabolism , Saliva/enzymology , Humans , Parotid Gland/enzymology , Protease Inhibitors , Submandibular Gland/enzymologyABSTRACT
After partial or total removal of salivary glands, parotid glands secreted practically the whole amount of alpha-amylase, DN-ase, and major portion of RN-ase, the submandibular glands providing more than 2/3 of the whole production of salivain. Comparison of output of enzymes with or without pilocarpin stimulation showed parotid glands to be the glands with periodical secretion and submandibular glands--with permanent secretion.
Subject(s)
Parotid Gland/metabolism , Saliva/enzymology , Submandibular Gland/metabolism , Amylases/metabolism , Animals , Deoxyribonucleases/metabolism , Female , Male , Organ Specificity , Peptide Hydrolases/metabolism , Pilocarpine/pharmacology , Rats , Ribonucleases/metabolismSubject(s)
Gastric Mucosa/drug effects , Kallikreins/physiology , Animals , Bradykinin/pharmacology , Depression, Chemical , Dose-Response Relationship, Drug , Gastric Juice/metabolism , Gastric Mucosa/metabolism , Rats , Saliva/physiology , Secretory Rate/drug effects , Submandibular Gland/metabolismSubject(s)
Gastric Mucosa/metabolism , Kallikreins/pharmacology , Submandibular Gland/analysis , Animals , DogsABSTRACT
By means of in vivo microscopy the influence of human, rat, and hamster purified salivary kallikreins upon the microvessels was studied in rat mesentery and hamster cheek pouch. Dilatation of arterioles, a decrease of the venule diameter, and an increase in the number of active capillaries was revealed. The species and organ peculiarities of these effects were described. The mesentery and the cheek pouch homogenates, albumin proteins, histamine and some amino acids were capable of activating the salivary kallikreins.
Subject(s)
Kallikreins/pharmacology , Mesentery/blood supply , Microcirculation/drug effects , Mouth Mucosa/blood supply , Saliva/analysis , Animals , Bradykinin/pharmacology , Cheek , Cricetinae , Humans , Kallikreins/analysis , RatsABSTRACT
Two kallikreins (K-I and K-II) were purified from mixed, parotid and submandibular human saliva. The kallikreins were separated by chromatography on CM-cellulose. The pH optima of activity were at pH 9.3 and pH 9.6-9.8; Km for BAEE was 1.10-3M and 4.10-3M, respectively. The esterase activity of K-I and K-II was inhibited by trasylol-like inhibitors, while the plant and synthetic inhibitors of trypsin were uneffective. In dog, rabbit and rat the hypotensive effect of K-II and its action upon the permeability of rabbit skin was 4-5 fold higher than the effects of K-I. Ki and K-II did not alter the arterial blood pressure in guinea pig.