Effect of high-molecular-weight component of Cranberry on plaque and salivary Streptococcus mutans counts in children: An in vivo study

A high molecular weight component of a saline extract derived from Listeria monocytogenes contained amino acids, carbohydrates, and phosphorus. The same fraction was capable of promoting both the in vitro mitogenic and adjuvant activities and the in vivo immunosuppressive activity displayed by the crude extract. The material was mitogenic to B but not to T lymphocytes in vitro. Responses to sheep and horse erythrocytes as well as to lipopolysaccharide were suppressed. Immunosuppression was dose dependent and was present at 1, 2, or 3 days but absent 7 days after injection. Both primary and secondary responses to sheep erythrocytes were impaired.

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Linear and high-molecular-weight poly-porphyrins for efficient photodynamic therapy

Biomaterials Science ◽

10.1039/d1bm00117e ◽

2021 ◽

Author(s):

Nan Zheng ◽

Xiahui Li ◽

Shangwei Huangfu ◽

Kangkai Xia ◽

Ruofei Yue ◽

...

Keyword(s):

Molecular Weight ◽

Photodynamic Therapy ◽

Quantum Yield ◽

Singlet Oxygen ◽

High Molecular Weight ◽

Linear Poly ◽

High Molecular Weight Poly

A linear poly-porphyrin with high Mw and conjugated by PEG and acetazolamide was developed with enhanced singlet oxygen quantum yield, improved photo-toxicity and excellent in vivo photodynamic therapy.

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Identification of two intermediates during processing of profilaggrin to filaggrin in neonatal mouse epidermis.

The Journal of Cell Biology ◽

10.1083/jcb.99.4.1372 ◽

1984 ◽

Vol 99 (4) ◽

pp. 1372-1378 ◽

Cited By ~ 59

Author(s):

K A Resing ◽

K A Walsh ◽

B A Dale

Keyword(s):

Molecular Weight ◽

High Molecular Weight ◽

Tandem Repeats ◽

Peptide Mapping ◽

Two Dimensional ◽

Major Event ◽

Mouse Epidermis ◽

Cell Stage ◽

Processing Steps

A major event in the keratinization of epidermis is the production of the histidine-rich protein filaggrin (26,000 mol wt) from its high molecular weight (greater than 350,000) phosphorylated precursor (profilaggrin). We have identified two nonphosphorylated intermediates (60,000 and 90,000 mol wt) in NaSCN extracts of epidermis from C57/Bl6 mice by in vivo pulse-chase studies. Results of peptide mapping using a two-dimensional technique suggest that these intermediates consist of either two or three copies of filaggrin domains. Each of the intermediates has been purified. The ratios of amino acids in the purified components are unusual and essentially identical. The data are discussed in terms of a precursor containing tandem repeats of similar domains. In vivo pulse-chase experiments demonstrate that the processing of the high molecular weight phosphorylated precursor involves dephosphorylation and proteolytic steps through three-domain and two-domain intermediates to filaggrin. These processing steps appear to occur as the cell goes through the transition cell stage to form a cornified cell.

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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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The interrelations between high- and low-molecular-weight forms of normal and mutant (Krabbe-disease) galactocerebrosidase

Biochemical Journal ◽

10.1042/bj1890009 ◽

1980 ◽

Vol 189 (1) ◽

pp. 9-15 ◽

Cited By ~ 11

Author(s):

Yoav Ben-Yoseph ◽

Melinda Hungerford ◽

Henry L. Nadler

Keyword(s):

Molecular Weight ◽

High Molecular Weight ◽

Specific Activity ◽

Polyacrylamide Gel Electrophoresis ◽

Active Form ◽

Sodium Dodecyl ◽

Krabbe Disease ◽

Low Molecular Weight ◽

Molecular Weight Form

Galactocerebrosidase (β-d-galactosyl-N-acylsphingosine galactohydrolase; EC 3.2.1.46) activity of brain and liver preparations from normal individuals and patients with Krabbe disease (globoid-cell leukodystrophy) have been separated by gel filtration into four different molecular-weight forms. The apparent mol.wts. were 760000±34000 and 121000±10000 for the high- and low-molecular-weight forms (peaks I and IV respectively) and 499000±22000 (mean±s.d.) and 256000±12000 for the intermediate forms (peaks II and III respectively). On examination by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, the high- and low-molecular-weight forms revealed a single protein band with a similar mobility corresponding to a mol.wt. of about 125000. Antigenic identity was demonstrated between the various molecular-weight forms of the normal and the mutant galactocerebrosidases by using antisera against either the high- or the low-molecular-weight enzymes. The high-molecular-weight form of galactocerebrosidase was found to possess higher specific activity toward natural substrates when compared with the low-molecular-weight form. It is suggested that the high-molecular-weight enzyme is the active form in vivo and an aggregation process that proceeds from a monomer (mol.wt. approx. 125000) to a dimer (mol.wt. approx. 250000) and from the dimer to either a tetramer (mol.wt. approx. 500000) or a hexamer (mol.wt. approx. 750000) takes place in normal as well as in Krabbe-disease tissues.

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Complex Formation of Covalently Crosslinked Fibrin Oligomers with Agarose Coupled Fibrinogen and Fibrin

10.1055/s-0039-1682429 ◽

1977 ◽

Author(s):

R. von Hugo ◽

R. Hafter ◽

A. Stemberger ◽

H. Graeff

Keyword(s):

Molecular Weight ◽

Complex Formation ◽

Affinity Chromatography ◽

High Molecular Weight ◽

Calcium Chloride ◽

Gel Filtration ◽

Void Volume ◽

Soluble Fibrin ◽

Derivatives Of

Crosslinked high molecular weight derivatives of fibrin (fibrinoligomers) were observed during intravascular coagulation. It was the purpose of this study to investigate the complex formation of fibrin oligomers with fibrinogen and fibrinmonomer. Fibrinogen coupled to agarose (Fg-ag) as well as fi-brinmonomer coupled to agarose (Fm-ag) was used as substrate. Soluble oligomers of fibrin were produced by incubating fibrinogen with thrombin, calcium-chloride, cystein and F XIII. They were separated from fibrinogen by gel filtration. Γ-dimers were demonstrated in fractions from the void volume and the shoulder prior to the fibrinogen peak. These fractions were subjected to affinity chromatography. Crosslinked oligomers of fibrin were not adsorbed on Fg-ag, yet adsorption occured on Fm-ag. This indicates that fibrin oligomers have no affinity to fibrinogen, yet readily form complexes with fibrin. This could mean that in vivo they compete with fibrinogen for the fibrinmonomer part of soluble fibrin monomer complexes, and hence have a tendency to increase in size.

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Immunological Properties of a High Molecular Weight Component from Yeast Cell Autolysate in Dogs and Evaluation of Its Potential Role in Human Dextran Reactions

European Surgical Research ◽

10.1159/000127953 ◽

1977 ◽

Vol 9 (5) ◽

pp. 338-346 ◽

Cited By ~ 5

Author(s):

J. Ring ◽

H. Hedin ◽

W. Richter ◽

F. Jesch ◽

K. Messmer

Keyword(s):

Molecular Weight ◽

Yeast Cell ◽

High Molecular Weight ◽

Potential Role ◽

Immunological Properties ◽

High Molecular Weight Component

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In Vitro and in Vivo Antigen-Induced Release of High-Molecular Weight Neutrophil Chemotactic Activity from Human Nasal Tissue

American Journal of Rhinology ◽

10.2500/105065888781693221 ◽

1988 ◽

Vol 2 (1) ◽

pp. 7-11 ◽

Cited By ~ 4

Author(s):

T. Nagakura ◽

T. Onda ◽

Y. likura ◽

T. Endo ◽

H. Nagakura ◽

...

Keyword(s):

Molecular Weight ◽

High Molecular Weight ◽

Nasal Polyps ◽

Gel Filtration ◽

Chemotactic Activity ◽

Nasal Tissue ◽

Nasal Secretions ◽

Neutrophil Chemotactic Activity

High molecular weight neutrophil chemotactic activity has been identified in resected human nasal polyps, inferior turbinates, and nasal secretions following antigen challenge. The estimated molecular weight, by gel filtration chromatography, was approximately 600,000. However, a heterogeneity of molecular weight in some patients was recognized. Our results suggest a possible role for high molecular weight-neutrophil chemotactic activity in the pathogenesis of hypersensitivity in the human nasal cavity.

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