Conditions influencing the synthesis of alkaline proteinases by Mucor microsporus Nam.

Bogusław Narzymski; Jadwiga Chmielnicka; Henryk Urbanek

doi:10.5586/am.1974.010

Conditions influencing the synthesis of alkaline proteinases by Mucor microsporus Nam.

Acta Mycologica ◽

10.5586/am.1974.010 ◽

2014 ◽

Vol 10 (2) ◽

pp. 295-304

Author(s):

Bogusław Narzymski ◽

Jadwiga Chmielnicka ◽

Henryk Urbanek

Keyword(s):

Proteolytic Activity ◽

Culture Filtrate ◽

Alkaline Proteinases

Maximal proteolytic activity at pH 8 was noted in the culture filtrate from Mucor microsorus when the medium contained: 30 g maltose, 10 g pepsine peptone, 5 g CaCO3, 1 g KN2PO4, 0.5 g MgSO4 7H2O, 0.5 g KCL, 0.05 g FeSO4, 0.05 g ZnSO4, 0.05 g MnCl2 in 1l.water.

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Peptocoagulase: clotting factor produced by bovine strains of Peptococcus indolicus

Journal of Clinical Microbiology ◽

10.1128/jcm.7.4.361-367.1978 ◽

1978 ◽

Vol 7 (4) ◽

pp. 361-367

Author(s):

L M Switalski ◽

O Schwam ◽

C J Smyth ◽

T Wadström

Keyword(s):

Proteolytic Activity ◽

Culture Filtrate ◽

Esterase Activity ◽

Methyl Esters ◽

Cell Suspensions ◽

Clinical Isolates ◽

Clotting Factor ◽

Stable Complex ◽

Washed Cell ◽

Stoichiometric Reaction

The production of a clotting factor (peptocoagulase) by bovine clinical isolates of Peptococcus indolicus and its nature were investigated. Extracellular peptocoagulase was demonstrated in culture filtrates of 93% and cell associated with washed cell suspensions of 100% of the 75 isolates tested. Both citrated and heparinized plasma were clotted. Crude peptocoagulase was nondialyzable, precipitated with (NH4)2SO4 at 40% saturation, somewhat resistant to heating at both neutral and acid pH, and chloroform insoluble. Culture filtrate did not contain proteolytic activity with albumin and casein, as substrates and no esterase activity was detected with tosylarginine and benzoylarginine methyl esters as substrates. The clotting reaction required peptocoagulase, prothrombin, and fibrinogen. The activation of prothrombin appeared to involve a stoichiometric reaction with peptocoagulase, possibly by formation of a stable complex.

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Immunologic significance of a collagen-derived culture filtrate containing proteolytic activity in -related diseases

Journal of Allergy and Clinical Immunology ◽

10.1016/0091-6749(94)90257-7 ◽

1994 ◽

Vol 93 (4) ◽

pp. 768-778 ◽

Cited By ~ 31

Author(s):

J TOMEE ◽

H KAUFFMAN ◽

A KLIMP ◽

J DEMONCHY ◽

G KOETER ◽

...

Keyword(s):

Proteolytic Activity ◽

Culture Filtrate

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Sem Observations in Gastric Mucosa Exposed to Progressive Enzymatic Etching

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s1431927600002531 ◽

1980 ◽

Vol 38 ◽

pp. 570-571

Author(s):

C.A.E. Lemmi ◽

D. Booth ◽

G.E. Adomian

Keyword(s):

Gastric Mucosa ◽

Critical Point ◽

Proteolytic Activity ◽

Etching Process ◽

Cellular Types

In order to enrich populations of homogeneous cellular types we dissociated gastric mucosa by enzymatic techniques. In addition, we used SEM to monitor the progressive etching of the mucosa. Two enzymes were tested: collagenase III with minimum proteolytic activity and Pronase with broader proteolytic effects. The gastric mucosa was exposed to the effect of the enzymes using everted stomach preparations. In this way the digestive action occured progressively from the lumen of the stomach toward the base of the glands. This “etching” process could be monitored conveniently by SEM. After incubation for periods varying from 30 to 210 minutes the tissues were stretched on dental wax, fixed in 2 % glutaralheyde, post-fixed in osmium, dehydrated, critical point dryed and coated with gold. A model MSM-5 “Mini-SEM” was used for observation. Gentle uncurling of the preparation before coating with gold produced fractures which revealed the structure of the gastric glandsin more detail.

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Mechanisms of Signaling through Urokinase Receptor and the Cellular Response

Thrombosis and Haemostasis ◽

10.1055/s-0037-1615847 ◽

1999 ◽

Vol 82 (08) ◽

pp. 305-311 ◽

Cited By ~ 31

Author(s):

Yuri Koshelnick ◽

Monika Ehart ◽

Hannes Stockinger ◽

Bernd Binder

Keyword(s):

Cell Surface ◽

Proteolytic Activity ◽

Tumor Invasion ◽

Cellular Response ◽

Transmembrane Protein ◽

Urokinase Receptor ◽

Biological Processes ◽

In Vivo Models ◽

Proteolytic Activation ◽

Core Proteins

IntroductionThe urokinase-urokinase receptor (u-PA-u-PAR) system seems to play a crucial role in a number of biological processes, including local fibrinolysis, tumor invasion, angiogenesis, neointima and atherosclerotic plaque formation, inflammation, and matrix remodeling during wound healing and development.1-6 Binding of urokinase to its specific receptor provides cells with a localized proteolytic potential. It stimulates conversion of cell surface-bound plasminogen into active plasmin, which, in turn, is required for proteolytic degradation of basement membrane components, including fibronectin, collagen, laminin, and proteoglycan core proteins.7 Moreover, plasmin activates other matrix-degrading enzymes, such as matrix metalloproteinases.8 Overexpression of u-PA/u-PAR correlates with tumor invasion and metastasis formation,9-13 while reduction of cell-surface bound u-PA and inhibition of u-PAR expression leads to a significant decrease of invasive and metastatic activity.14 Specific antagonists that suppress binding of u-PA to u-PAR have been shown to inhibit cell-surface plasminogen activation, tumor growth, and angiogenesis both in vitro and in vivo models.15,16 Independently of its proteolytic activity, u-PA is implicated in many biological processes that seem to require u-PAR-mediated intracellular signal transduction, such as proliferation, chemotactic movement and adhesion, migration, and differentiation.17 Data obtained in the late 1980s indicated that u-PA not only provides cells with local proteolytic activity, but might also be capable of transducing signals to the cell.18-22 At that time, however, the u-PAR has just been isolated, cloned, and identified as a glycosylphosphatidylinositol (GPI)-linked protein and not a transmembrane protein. Signaling via the u-PAR was, therefore, regarded as being unlikely, and the effects of u-PA on cell proliferation18-22 were thought to be mediated by proteolytic activation of latent growth factors. The assumption of direct signaling via u-PAR was, in fact, considered controversial, until about 10 years later when a physical association between u-PAR and signaling proteins was found.23 From this report on, several proteins associated with u-PAR have been identified. Now, u-PAR seems to be part of a large “signalosome” associated and interacting with several proteins on both the outside and inside of the cell.

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A New Method for Plasminogen Standardization

Thrombosis and Haemostasis ◽

10.1055/s-0038-1651297 ◽

1968 ◽

Vol 20 (03/04) ◽

pp. 548-554

Author(s):

J Gajewski ◽

G Markus

Keyword(s):

Proteolytic Activity ◽

Specific Activity ◽

Molar Ratio ◽

Sharp Transition ◽

Equivalence Point ◽

Constant Amount ◽

Residual Level ◽

Activity Measurements ◽

Complete Saturation ◽

Human Plasminogen

SummaryA method for the standardization of human plasminogen is proposed, based on the stoichiometric interaction between plasminogen and streptokinase, resulting in inhibition of proteolytic activity. Activation of a constant amount of plasminogen with increasing amounts of streptokinase yields linearly decreasing activities, as a function of streptokinase, with a sharp transition to a constant residual level. The point of transition corresponds to complete saturation of plasmin with streptokinase in a 1:1 molar ratio, and is therefore a measure of the amount of plasminogen present initially, in terms of streptokinase equivalents. The equivalence point is independent of the kind of protein substrate used, buffer, pH, length of digestion and, within limits, temperature. The method, therefore, is not subject to the variations commonly encountered in the usual determination based on specific activity measurements.

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Mechanism of Human Plasminogen Activation by Streptokinase and Human Plasmin

Thrombosis and Haemostasis ◽

10.1055/s-0038-1654808 ◽

1964 ◽

Vol 11 (01) ◽

pp. 085-093

Author(s):

W. F Blatt ◽

JL Gray ◽

H Jensen

Keyword(s):

Proteolytic Activity ◽

Low Ph ◽

Plasminogen Activation ◽

Sensitive Tool ◽

Human Plasminogen

SummaryA sensitive tool has been described for measuring fibrinolysis in reconstituted systems using thrombelastography. Activator mixtures with no appreciable proteolytic activity can similarly be tested in this system when the fibrinogen utilized has sufficient plasminogen present. Exposure of human plasminstreptokinase mixtures formed at pH 7.0 to acid conditions produced a striking loss of activator activity which could not be ascribed to low pH lability of the components, nor to plasmin action on the SK at pH 2.0. This is additional evidence for the hypothesis that human plasmin interacts with SK to form a complex capable of converting human and bovine plasminogen to plasmin.

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ВПЛИВ ДЖЕРЕЛ АЗОТНОГО ЖИВЛЕННЯ НА СИНТЕЗ КАРОТИНОЇДІВ ДЕЯКИМИ ШТАМАМИ БАЗИДІОМІЦЕТІВ

Biological Bulletin of Bogdan Chmelnitskiy Melitopol State Pedagogical University ◽

10.15421/20144_02 ◽

2014 ◽

Vol 4 (01) ◽

pp. 22

Author(s):

A. K. Veligodska ◽

O. V. Fedotov ◽

A. S. Petreeva

Keyword(s):

Culture Filtrate ◽

Nutrient Medium ◽

Culture Fluid ◽

Carotenoid Content ◽

Nitrogen Compounds ◽

Total Carotenoid ◽

Carotenoid Accumulation ◽

Total Carotenoid Content ◽

Peptone Medium ◽

Acetone Extracts

The influence of certain nitrogen compounds - components of glucose-peptone medium (GPM) on the accumulation of carotenoids by some strains was investigated by surface cultivating basidiomycetes. The total carotenoid content was set in acetone extracts of mycological material spectrophotometrically and calculated using the Vetshteyn formula. As the nitrogen-containing components used GPM with 9 compounds, such as peptone, DL-valine, L-asparagine, DL-serine, DL-tyrosine, L-proline, L-alanine, urea, NaNO3. The effect on the accumulation of specific compounds both in the mycelium and in the culture fluid of carotenoids by culturing certain strains of Basidiomycetes was identified. Adding to standard glucose-peptone medium peptone at 5 g/l causes an increase of carotenoid accumulation by strain L. sulphureus Ls-08, and in a concentration of 4 g/l by strains of F. hepatica Fh-18 and F. fomentarius Ff-1201. In order to increase the accumulation of carotenoids in the mycelium we suggested to make a standard glucose-peptone medium with proline or valine for cultivating of L. sulphureus Ls- 08 strain; alanine for F. fomentarius Ff-1201 strain; proline, asparagine and serine - for strain Fh-18 of F. hepatica. The results can be implemented in further optimization of the composition of the nutrient medium for culturing strains of Basidiomycetes wich producing carotenoids. Keywords: nitrogen-containing substances, Basidiomycetes, mycelium, culture filtrate, carotenoids

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