Alkaline proteinase localization in myoblasts.

Recent interest in elucidating the role of non-lysosomal proteases in intracellular protein catabolism in muscle has led to various investigations with three alkaline proteases: a trypsin-like, a chymotrypsin-like, and a high molecular weight cysteine proteinase. Although in vitro biochemical assays have revealed the catabolic potential of at least two of these proteases, confirmation of their presence in muscle cells has been difficult. In this study immunohistochemical techniques were employed to localize each of these proteases in rat myoblasts. Antisera against the trypsin-like and chymotrypsin-like proteinase (both serine proteinases) showed strong localization in the cytoplasm immediately around the nucleus. Both also stained chromatin material in the nucleus of these cells. Fluorescent localization of the high molecular weight cysteine proteinase (Proteinase I) also appeared to be cell-associated in the myoblasts. The use of myoblasts in cell culture sections of whole muscle was advantageous, since localization of the proteases could be assessed in the absence of other cell types.

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The Effect of Dextran of Various Molecular Weight on the Coagulation in Dogs

Thrombosis and Haemostasis ◽

10.1055/s-0038-1654535 ◽

1961 ◽

Vol 06 (01) ◽

pp. 015-024 ◽

Cited By ~ 32

Author(s):

Sven Erik Bergentz ◽

Oddvar Eiken ◽

Inga Marie Nilsson

Keyword(s):

Molecular Weight ◽

Body Weight ◽

High Molecular Weight ◽

Bleeding Time ◽

Factor Vii ◽

Low Molecular Weight ◽

Factor V ◽

Coagulation Mechanism ◽

Coagulation Defects

Summary1. Infusions of low molecular weight dextran (Mw = 42 000) to dogs in doses of 1—1.5 g per kg body weight did not produce any significant changes in the coagulation mechanism.2. Infusions of high molecular weight dextran (Mw = 1 000 000) to dogs in doses of 1—1.5 g per kg body weight produced severe defects in the coagulation mechanism, namely prolongation of bleeding time and coagulation time, thrombocytopenia, pathological prothrombin consumption, decrease of fibrinogen, prothrombin and factor VII, factor V and AHG.3. Heparin treatment of the dogs was found to prevent the decrease of fibrinogen, prothrombin and factor VII, and factor V otherwise occurring after injection of high molecular weight dextran. Thrombocytopenia was not prevented.4. In in vitro experiments an interaction between fibrinogen and dextran of high and low molecular weight was found to take place in systems comprising pure fibrinogen. No such interaction occurred in the presence of plasma.5. It is concluded that the coagulation defects induced by infusions of high molecular weight dextran are due to intravascular coagulation.

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Physicochemical and Antifungal Properties of Clotrimazole in Combination with High-Molecular Weight Chitosan as a Multifunctional Excipient

Marine Drugs ◽

10.3390/md18120591 ◽

2020 ◽

Vol 18 (12) ◽

pp. 591

Author(s):

Bożena Grimling ◽

Bożena Karolewicz ◽

Urszula Nawrot ◽

Katarzyna Włodarczyk ◽

Agata Górniak

Keyword(s):

Molecular Weight ◽

High Molecular Weight ◽

Weight Ratio ◽

Scanning Calorimetry ◽

Minimal Inhibitory Concentrations ◽

Dissolution Tests ◽

Effective Combination ◽

The Impact ◽

High Molecular Weight Chitosan

Chitosans represent a group of multifunctional drug excipients. Here, we aimed to estimate the impact of high-molecular weight chitosan on the physicochemical properties of clotrimazole–chitosan solid mixtures (CL–CH), prepared by grinding and kneading methods. We characterised these formulas by infrared spectroscopy, differential scanning calorimetry, and powder X-ray diffractometry, and performed in vitro clotrimazole dissolution tests. Additionally, we examined the antifungal activity of clotrimazole–chitosan mixtures against clinical Candida isolates under neutral and acid conditions. The synergistic effect of clotrimazole and chitosan S combinations was observed in tests carried out at pH 4 on Candida glabrata strains. The inhibition of C. glabrata growth reached at least 90%, regardless of the drug/excipient weight ratio, and even at half of the minimal inhibitory concentrations of clotrimazole. Our results demonstrate that clotrimazole and high-molecular weight chitosan could be an effective combination in a topical antifungal formulation, as chitosan acts synergistically with clotrimazole against non-albicans candida strains.

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Identity and Origin of the ATPase activity associated with neuronal microtubules. I. The ATPase activity is associated with membrane vesicles.

The Journal of Cell Biology ◽

10.1083/jcb.96.5.1298 ◽

1983 ◽

Vol 96 (5) ◽

pp. 1298-1305 ◽

Cited By ~ 13

Author(s):

D B Murphy ◽

R R Hiebsch ◽

K T Wallis

Keyword(s):

Molecular Weight ◽

Atpase Activity ◽

High Molecular Weight ◽

Brain Tissue ◽

Membrane Vesicles ◽

Microtubule Associated Proteins ◽

In Vitro Assembly ◽

Microtubule Protein ◽

Associated Proteins

Microtubule protein purified from brain tissue by cycles of in vitro assembly-disassembly contains ATPase activity that has been postulated to be associated with microtubule-associated proteins (MAPs) and therefore significant for studies of microtubule-dependent motility. In this paper we demonstrate that greater than 90% of the ATPase activity is particulate in nature and may be derived from contaminating membrane vesicles. We also show that the MAPs (MAP-1, MAP-2, and tau factors) and other high molecular weight polypeptides do not contain significant amounts of ATPase activity. These findings do not support the concept of "brain dynein" or of MAPs with ATPase activity.

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Interaction of Streptococcus mutans Glucosyltransferases with Teichoic Acids

Infection and Immunity ◽

10.1128/iai.29.2.376-382.1980 ◽

1980 ◽

Vol 29 (2) ◽

pp. 376-382

Author(s):

H. K. Kuramitsu ◽

L. Wondrack ◽

M. McGuinness

Keyword(s):

Molecular Weight ◽

High Molecular Weight ◽

Streptococcus Mutans ◽

Teichoic Acid ◽

Lipoteichoic Acid ◽

Water Soluble ◽

Heat Inactivation ◽

Teichoic Acids ◽

Insoluble Glucan

The Streptococcus mutans GS5 glucosyltransferase activities (both water-soluble and -insoluble glucan-synthesizing fractions) were inhibited by purified lipoteichoic acid. In vitro sucrose-dependent colonization of smooth surfaces by strain GS5 was also markedly reduced in the presence of the amphipathic molecules. The inhibition of soluble glucan synthesis by lipoteichoic acid appeared to be competitive with respect to both sucrose and primer dextran T10. These inhibitory effects were dependent on the presence of the fatty acid components of lipoteichoic acid since deacylated lipoteichoic acids did not inhibit glucosyltransferase activity. However, the deacylated molecules did interact with the enzymes since deacylated lipoteichoic acid partially protected the enzyme activity against heat inactivation and also induced the formation of high-molecular-weight enzyme complexes from the soluble glucan-synthesizing fraction. The presence of teichoic acid in high-molecular-weight aggregates of glucosyltransferase isolated from the culture fluids of strain GS5 was suggested by the detection of polyglycerophosphate in these fractions. In addition to strain GS5, two other organisms containing polyglycerophosphate teichoic acids, Lactobacillus casei and Lactobacillus fermentum , were demonstrated to bind glucosyltransferase activity. These results are discussed relative to the potential role of teichoic acid-glucosyltransferase interactions in enzyme binding to the cell surface of S. mutans and the formation of high-molecular-weight enzyme aggregates in the culture fluids of the organism.

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Preparation of high-molecular weight and high-sulfate content chitosans and their potential antioxidant activity in vitro

Carbohydrate Polymers ◽

10.1016/j.carbpol.2005.04.007 ◽

2005 ◽

Vol 61 (2) ◽

pp. 148-154 ◽

Cited By ~ 97

Author(s):

Ronge Xing ◽

Song Liu ◽

Huahua Yu ◽

Zhanyong Guo ◽

Zhien Li ◽

...

Keyword(s):

Molecular Weight ◽

Antioxidant Activity ◽

High Molecular Weight ◽

Sulfate Content ◽

High Sulfate

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Pro-angiogenic effect of human kallikrein-related peptidase 12 (KLK12) in lung endothelial cells does not depend on kinin-mediated activation of B2 receptor

Biological Chemistry ◽

10.1515/hsz-2012-0291 ◽

2013 ◽

Vol 394 (3) ◽

pp. 385-391 ◽

Cited By ~ 11

Author(s):

Thomas Kryza ◽

Gilles Lalmanach ◽

Marion Lavergne ◽

Fabien Lecaille ◽

Pascale Reverdiau ◽

...

Keyword(s):

Molecular Weight ◽

Endothelial Cells ◽

High Molecular Weight ◽

High Molecular Weight Kininogen ◽

Kinin Receptor ◽

Angiogenic Effect ◽

Lung Endothelial Cells ◽

Carboxy Terminal

Abstract Kallikrein-12 (KLK12) may play an important role in angiogenesis modulating proangiogenic factor bioavailability and activating the kinin receptor B2 pathway. We studied whether KLK12 had an impact on angiogenesis and the activation of kinin receptor B2 results from the KLK12-dependent generation of kinins. KLK12 efficiently hydrolyzed high molecular weight kininogen, liberating a fragment containing the carboxy-terminal end of kinins. The kininogenase activity of KLK12 was poor, however, due to the cleavage resistance of the N-terminal side of the kinin sequence. A very low amount of kinins was accordingly released after in vitro incubation of high molecular weight kininogen with KLK12 and thus the proangiogenic activity of KLK12 in lung endothelial cells was not related to a kinin release.

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Rat platelets activate high molecular weight atrial natriuretic peptides in vitro.

Hypertension ◽

10.1161/01.hyp.7.6.905 ◽

1985 ◽

Vol 7 (6_pt_1) ◽

pp. 905-912 ◽

Cited By ~ 8

Author(s):

N C Trippodo ◽

A Januszewicz ◽

B L Pegram ◽

F E Cole ◽

N Kohashi ◽

...

Keyword(s):

Molecular Weight ◽

High Molecular Weight ◽

Natriuretic Peptides ◽

Atrial Natriuretic Peptides ◽

Rat Platelets ◽

Atrial Natriuretic

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PHOTOCHEMISTRY OF HIGH MOLECULAR WEIGHT PHYTOCHROME IN VITRO

Photochemistry and Photobiology ◽

10.1111/j.1751-1097.1975.tb06717.x ◽

1975 ◽

Vol 22 (1-2) ◽

pp. 33-36 ◽

Cited By ~ 60

Author(s):

Lee H. Pratt

Keyword(s):

Molecular Weight ◽

High Molecular Weight

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In Vitro Antioxidant Activity and FTIR Characterization of High-Molecular Weight Melanoidin Fractions from Different Types of Cocoa Beans

Antioxidants ◽

10.3390/antiox8110560 ◽

2019 ◽

Vol 8 (11) ◽

pp. 560 ◽

Cited By ~ 6

Author(s):

Oracz ◽

Zyzelewicz

Keyword(s):

Molecular Weight ◽

High Molecular Weight ◽

Antioxidant Properties ◽

Model Systems ◽

Total Phenolic ◽

Cocoa Beans ◽

Potential Health ◽

Antioxidant Power ◽

Different Types

Melanoidins from real foods and model systems have received considerable interest due to potential health benefits. However, due to the complexity of these compounds, to date, the exact structure of melanoidins and mechanism involved in their biological activity has not been fully elucidated. Thus, the aim of this study was to investigate the total phenolic content, antioxidant properties, and structural characteristics of high-molecular weight (HMW) melanoidin fractions isolated by dialysis (>12.4 kDa) from raw and roasted cocoa beans of Criollo, Forastero, and Trinitario beans cultivated in various area. In vitro antioxidant properties of all studied HMW cocoa fractions were evaluated by four different assays, namely free radical scavenging activity against DPPH● and ABTS●+ radicals, ferric reducing antioxidant power (FRAP), and metal-chelating ability. Additionally, the structure–activity relationship of isolated HMW melanoidin fractions were analyzed using attenuated total reflectance Fourier transform infrared spectroscopy (ATR-FTIR). The results show that roasting at a temperature of 150 °C and a relative air humidity of 0.3% effectively enhances the total phenolics content and the antioxidant potential of almost all HMW cocoa melanoidin fractions. The ATR-FTIR analysis revealed that the various mechanisms of action of HMW melanoidins isolates of different types of cocoa beans related to their structural diversity. Consequently, the results clearly demonstrated that HMW cocoa fractions isolated from cocoa beans (especially those of Criollo variety) roasted at higher temperatures with the lower relative humidity of air possess high antioxidant properties in vitro.

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