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At least 145 records · Page 8Linked to original sources
PubMed1977

Serial enzymatic hydrolysis of cell walls of two serotypes of yeast-form Histoplasma capsulatum with alpha(1 leads to 3)-glucanase, beta(1 leads to 3)-glucanase, pronase, and chitinase.

A serial enzymatic hydrolysis procedure for the partial lysis of Histoplasma capsulatum yeast-form cell walls was described, and its application for the differentiation of two serotypes was evaluated. Cell walls were serially digested with alpha(1 leads to 3)-glucanase and beta(1 leads to 3)-glucanse of Cladosporium resinae, then by Pronase, and then by chitinase. The walls of serotype 1, 2, 3 (61.5% digested) were not susceptible to alpha(1 leads to 3)-glucanse, and they contained 30.3% chitin, thus identifying the strain as chemotype 1 (chem 1). Serotype 1, 4 cells walls (51.6% digested) released 27.3% as glucose after treatment with alpha(1 leads to 3)-glucanse and contained 7.8% chitin, compatible with chemotype 2 (chem 2). In addition to quantitating the monomeric products of enzymolysis, I recovered soluble nondialyzable polysaccharide from the digests of both serotypes.

Cell Wall↗
PubMed1988

Enzyme-linked immunosorbent assay of antibody to group A Streptococcus-specific C carbohydrate with trypsin-pronase-treated whole cells as antigen.

We describe the measurement by enzyme-linked immunosorbent assay of antibody to group A Streptococcus C carbohydrate in immunized rabbits and human sera, with trypsin-pronase-treated group A streptococcal whole cells used as the antigen. The optimal concentration of the enzyme-treated whole cells used to coat the wells was 2 x 10(7) cells per well. Rabbit antiserum diluted to 1:12,800 and human serum diluted to 1:1,000 were found to be the optimal concentrations for antibody measurement. Antibody that reacted with enzyme-treated whole cells in rabbit antiserum was absorbed with group A streptococcal whole cells, purified C carbohydrate, and N-acetylglucosamine only. Enzyme-treated whole cells did not react with anti-lipoteichoic acid antibody, and rabbit antiserum did not react with lipoteichoic acid. There was a highly significant correlation between the anti-C carbohydrate antibody titrated with enzyme-treated whole cells and that with purified C carbohydrate as antigen. The correlation coefficient for the immunoglobulin M (IgM) antibodies was r = 0.75, and for the IgG antibodies it was r = 0.77. When the IgG antibody titers to the enzyme-treated whole cells of the sera of patients with acute poststreptococcal glomerulonephritis and rheumatic fever were compared with those of sera of healthy individuals, the sera of patients with poststreptococcal sequelae had significantly higher titers than did healthy individuals. Although anti-C carbohydrate antibody in human sera mostly belonged to the IgG2 subclass, there was anti-C carbohydrate antibody that belonged to the IgG3 subclass in a certain percentage of patients with rheumatic fever and acute poststreptococcal glomerulonephritis.

Adolescent↗
PubMed1979

Localisation of the changes of the sensitivity of the airways by proteolytic enzymes (pronase) against acetylcholine.

Proteolytic enzymes increase the sensitivity of the bronchial system against acetylcholine when inhaled as aerosols. These experiments were performed on 33 dogs in order to localize the area of sensitivity in the bronchial system responsible fe aerosol only to the upper part of the airtract sensitises the lower part of the airways against acetylcholine. Pronase aerosol given to the lower part of the airways needs higher dosages for sensitization to acetylcholine. This effect assumes an interaction between the upper sensoric part in the reflex way of airway obstruction and the lower airways. Changes caused by proteolytic enzymes in the upper part of the airtract can cause increased reactivity of the lower airways.

Acetylcholine↗
PubMed1999

Preparation of gastric mucin "STP-domains" using pronase digestion and chemical deglycosylation.

In this work we present a method of mucin protein backbone fragments preparation, which are rich in serine, threonine and proline amino acid residues. The purified native gastric mucin was reduced, the pronase digested and chemically deglycosylated. The obtained apomucin preparations contained slight quantities of residual carbohydrates (0-1%). In O-glycosylation reaction in vitro, with the participation of GalNAc-transferase, the amounts of incorporated [14C]GalNAc to apomucin fractions were about twofold greater in relation to the deglycosylated non-digested mucin subunits. We also demonstrate the usefulness of immunoblotting technique of apomucin preparations detection.

Electrophoresis, Polyacrylamide Gel↗
PubMed1975

Laboratory model of membranous glomerulonephritis in rats induced by pronase-digested homologous renal tubular epithelial antigen.

The laboratory counterpart of tubular antigen-mediated membranous glomerulonephritis in humans was produced in rats by a single injection of homologous nephritogenic tubular antigen with adjuvant. The rat developed membranous glomerulonephritis with typical clinicopathologic features of human nephritis mediated by the tubular antigen, i.e., massive proteinuria and diffuse thickening of glomerular basement membranes due to deposition of tubular antigen-antibody complexes which were demonstrated by immunofluorescent technique. The nephritogenic tubular antigen was solubilized by pronase digestion, further purified by gel filtration, and demonstrated to have the same physicochemical properties as the human tubular antigen which was found in the deposits together with beta1C- and immunoglobulins in the glomeruli of patients with membranous glomerulonephritis.

Animals↗
PubMedDate not supplied

[Pronase E and P immobilization on aminoorganosilica surface].

Immobilization of pronase E and P was performed on sylochrome modified by gamma-aminopropyltrietoxysilane using cyanuric chloride, 2,4--toluylenediisocyanate, glutaric aldehyde and also on sylochrome by means of titanium tetrachloride. The esterase and caséinolytic activities of the immobilized preparations and their stability during storage were determined. The increased thermostability of the immobilized preparation is established. The influence of the enzyme: carrier ratio on the immobilization process and activity of the enzymes was studied. It is shown that application of glutaric aldehyde favours the best retention of the esterase activity (73%), whereas the caseinolytic activity is better retained (31%) when titanium tetrachloride was used.

Drug Stability↗
PubMed1990

Lectin binding in murine tumour lines with different malignant characteristics. Effect of enzyme (pronase, neuraminidase) treatment on lectin labelling.

We used 5 syngeneic murine tumour systems for studying quantitative lectin surface binding of intact viable tumour cells. We also investigated, for 3 of the tumours, whether the lectin binding sites were susceptible to proteolytic enzyme (pronase) or neuraminidase treatment. There were significant differences between two of the tumour lines in the binding of wheat germ agglutinin (WGA), concanavalin A (ConA). peanut agglutinin (PNA), soybean agglutinin (SBA) and Ulex europeus agglutinin (UEA). There were also variations in lectin binding between the other tumor lines, but these differences were not statistically significant. Lectin binding showed no evident relationship to the malignancy or the metastasis-forming capacity of the respective tumour cell line. Proteolytic treatment, which drastically affects intravenously induced experimental metastasis formation by one of the tumours, caused a decreased binding of SBA, ConA and WGA. Neuraminidase treatment increased both PNA and SBA binding in three different cell lines, presumably by removing sialic acid masking D-galactose and N-acetyl-D-galactose-amine groups.

Animals↗
PubMedDate not supplied

[Modification of latrotoxin channels under the effect of pronase and antibodies to latrotoxin].

The action of pronase and latrotoxin antibodies on alpha-latrotoxin channels in lipid bilayers has been investigated. Proteolysis of the protruding portions of the inserted channels changed slightly its conductivity and selectivity. Latrotoxin antibodies added to either side of the membrane decreased channel conductivity. The effect depends on the membrane potential. It is suggested that the channel conformation depends on the transmembrane potential and selective centre localized in the inner region of a bilayer is insensitive to proteolysis of protruding segments.

Antibodies↗
PubMed1986

High and low affinity receptors for interleukin 2: implications of pronase, phorbol ester, and cell membrane studies upon the basis for differential ligand affinities.

Cellular binding sites for IL 2 exist in two forms which differ with respect to their apparent affinity for the factor. The present studies were designed to evaluate various models for the difference. Receptor-mediated internalization and covalent receptor-ligand coupling were discounted as explanations on the basis of ligand binding and elution studies on permeabilized cells and cell membranes. Phosphorylation of the receptor during activation of protein kinase C failed to modulate the ratio of high and low affinity sites, demonstrating that it also did not provide a potential mechanism. Selective destruction of low affinity receptors with pronase, on the other hand, indicated that the two forms of binding sites differed significantly in their cell surface structure. Either the two types of receptor consist of distinct molecules or the conformation of the high affinity binding sites renders them more resistant to proteolysis. Antibody inhibition studies revealed that the high affinity receptors remaining after protease treatment and their low affinity counterparts both utilized the same ligand-binding component. Thus, this result ruled out the possibility of two totally distinct receptor structures. Together, the findings support the hypothesis that other membrane components modify the conformation of the ligand-binding polypeptide to confer a high affinity protease-resistant configuration.

Antibodies, Monoclonal↗
PubMed1988

Characteristics of two malignant lymphomas in C57B1/6J mice. Cytogenetic changes and the distribution of i.v. transfused tumor cells with and without enzyme (pronase, neuraminidase) treatment.

Two T-cell lymphomas induced by a combination of antigen stimulation and immunosuppression in inbred C57Bl/6J mice, BWL1 and BWL2 (Ryd et al. 1985), were further characterized. Cytogenetically they have the same trisomy 15 abnormality as chemically, virally and radiation induced T-cell lymphomas. Analyses of early and late tumour generations indicate that both tumours are chromosomally stable. After i.v. transplantation, the two tumors grew in a similar manner and preferentially in spleen and liver. Proteolytic treatment of the tumor cells changed the distribution of both lymphomas from the lungs to other organs. Neuraminidase treatment had no such effect on BWL2, but a similar but weaker effect than pronase on BWL1. Our findings support the notion that the distribution of lymphomas are, at least in part, governed by cell-surface characteristics.

Animals↗
PubMed1987

Solubilization of porcine zonae pellucidae by trypsin and pronase.

The porcine zona pellucida was dissolved with difficulty by trypsin in isotonic solution, whereas it was efficiently dissolved by pronase. A structural change of the zona was induced in hypotonic solution, resulting in acceleration of dissolution by these proteases. The solubilization rate of three families (PZP1-3) of zona protein by both enzymes was analyzed by HPLC. In hypotonic solution, PZP1 was solubilized first, followed by PZP2; and PZP3 was then finally released. In isotonic solution, PZP1 and PZP2 were also solubilized faster than PZP3, which was almost completely resistant to trypsin, showing that the solubilization of the zona depended on that of PZP3. Noticeably, high molecular weight products were produced as the proteolytic hydrolysis proceeded in PBS. Circular dichroic spectra and electrophoretograms of the tryptic hydrolysates showed that the zona may have a regular supramolecular structure.

Animals↗
PubMed1980

The use of pronase enhances sensitivity of the PAP method in the detection of intracytoplasmic immunoglobulins.

Application of immunocytochemistry to formalin-fixed, paraffin-embedded material tends to provide capricious results, even when employing the unlabelled antibody peroxidase-antiperoxidase (PAP) method. This study shows that treatment of tissue sections with pronase, a protease isolated from a strain of Streptomyces griseus, prior to performance of the PAP procedure greatly enhances its sensitivity. The optimum conditions for use of this enzyme in detecting intracellular immunoglobulins are given.

Humans↗
PubMedDate not supplied

[Molecular organization of the long-wave complexes of purple photosynthesizing bacteria. Effect of pronase on the B890 complex of Chromatium minutissium and Rhodopseudomonas palustris].

The pronase action on the long-wave complexes B890 from two different purple bacteria has been investigated. Differences in the kinetics of decrease of the reaction center photochemical activity of electron-donor activity of cytochromes and of destruction of Bx890 (875) forms have been discovered. Different rates of the proteolysis of RC proteins were revealed by SDS-gel-electrophoresis. The heavy protein of RC was the first to degrade. The photochemical transformations deltaA890(875) in B890 complexes was observed during formation of peptides with molecular weight about 17 000 from two other RC proteins. On the basis of obtained data the model of molecular organization of B890 complexes from purple bacteria is discussed.

Bacterial Chromatophores↗
PubMed1998

Loading of intact rabbit erythrocytes with fluorophores and the enzyme pronase by means of electroporation.

The application of electric field pulses in cell suspensions is known to alter membrane integrity, resulting in increased membrane permeabilization. This field-induced membrane poration provides the means to load cells with a variety of external substances, useful for clinical applications. In this work, intact rabbit erythrocytes were successfully loaded with low molecular weight fluorescent probes and with the high molecular weight enzyme pronase, which has been shown to mimic the effects of insulin. Attachment of the enzyme onto the cell surface was also achieved by modifying the applied pulse parameters. Both applications were efficient and accompanied by high cell survival rates. In this way, biological carriers loaded with active substances were produced, offering the potentials for useful clinical applications, either for diagnostic or therapeutic purposes.

Animals↗
PubMed1984

Removal of swine zonae pellucidae with sequential exposures to pronase and acidified medium.

Exposure to acidified PBS (pH 3) for 60 sec removed swine zonae pellucidae from 70.4% of 27 swine morulae, and 73.7% of these formed blastocysts in culture. Further investigations revealed that treating embryos with 0.5% pronase and acidified PBS (pH 3) for 30 sec each was more effective. Zonae were removed in 90.6% of 85 embryos (four-cell to morulae) treated. A total of 76.9% of 65 zona-free embryos and 81.6% of 38 untreated embryos formed blastocysts (P>0.05). An additional 57 untreated and 49 zona-free embryos (morulae to blastocysts) were transferred to seven recipient sows. Four sows returned to estrus (18 to 27 days), but three others were pregnant when slaughtered at 38 to 42 days. One pregnant sow had received a combination of five zona-free and six untreated embryos and demonstrated the potential for further development of treated embryos in vivo.

Journal Article↗
PubMed1970

The specificity of proteinases from Streptomyces griseus (pronase).

Purification of pronase by ion-exchange chromatography gave four proteolytically active fractions. Fraction A(2) contained an endopeptidase that attacks poly l-valine. Fraction B contained an endopeptidase, an aminopeptidase and carboxypeptidases. The activities against hippuryl-l-arginine and hippuryl-l-phenylalanine could be inhibited to a considerable extent by di-isopropyl phosphorofluoridate and by EDTA. Fraction C contained an endopeptidase resembling bovine trypsin. The pure enzyme was completely inactivated by di-isopropyl phosphorofluoridate and pancreatic trypsin inhibitor and to about 90% by other naturally occurring trypsin inhibitors. Fraction D contained an apparently homogeneous endopeptidase, inhibited by diisopropyl phosphorofluoridate, that adsorbed to and hydrolysed elastin. The activity of all these fractions was tested qualitatively against a wide range of small peptides and synthetic substrates.

Aminopeptidases↗
PubMed1970

Preparation, properties and substrate-exclusion effects of an insoluble pronase derivative.

1. A diazotized co-polymer of leucine and p-aminophenylalanine was used to prepare insoluble pronase. 2. The product was similar to the native enzyme in pH optimum, temperature optimum and broad specificity. 3. Exclusion effects were observed that appear related to the molecular weight of the substrate being hydrolysed. 4. The effects are explained on the basis of impedance of substrate access to the catalytic site by the supporting solid matrix.

Albumins↗