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D Moe

Publications and source records attributed to D Moe.

At least 37 records · Page 2Linked to original sources
PubMed1990

Electrophoretic demonstration of glycoproteins, lipoproteins, and phosphoproteins in human and bovine enamel.

Enamel proteins from fully mineralized human molars and from bovine tooth germs were separated by electrophoresis. The gels were stained for detection of glycoproteins, lipoproteins, and phosphoproteins. Glycoproteins were shown by periodic acid-Schiff staining and lectin blotting. In mature human enamel a number of high molecular weight proteins could be demonstrated after ethylenediaminetetra-acetic acid demineralization and subsequent Triton X-100 extraction. These proteins are suggested to be lipoproteins. Phosphoproteins could only be visualized in enamel matrix from the tooth germs.

Animals↗
PubMed1990

Non-specific esterases in partly mineralized bovine enamel.

Activity for non-specific esterase was demonstrated in the matrix of developing bovine enamel with alpha-naphthyl acetate and 5-bromoindoxyl acetate as the esterase substrates. By use of high-performance liquid chromatography gel filtration, ion-exchange chromatography, and electrophoresis three esterases were shown to be present in the enamel matrix. The enzymes showed highest activity at pH 6.5-7.5. In sections a strong reaction was observed in the secretory ameloblasts. The esterases may be proteolytic enzymes that participate in the degradation of the matrix proteins.

Amelogenesis↗
PubMed1989

Non-specific esterases and esterproteases in masticatory muscles from the muscular dystrophic mouse.

With the aid of histochemical and electrophoretic techniques activities for esterase and esterprotease were investigated in the digastric and masseter muscles from normal and dystrophic mice. The substrates used were alpha-naphthyl acetate and N-acetyl-L-alanine alpha-naphthyl ester. According to the microscopic observations of the dystrophic muscles the histopathological changes in the masseter muscle were much more pronounced than in the digastric muscle. The connective tissue surrounding the myofibers of the dystrophic masseter contained a large number of cells with pronounced enzyme activity. Among them were mast cells that were strongly stained for esterprotease. The connective tissue of the dystrophic digastricus was much less infiltrated with cellular elements reacting for esterprotease. In zymograms the normal digastricus, the dystrophic masseter and the dystrophic digastricus showed a strong activity for certain isoenzymes that were absent or weakly expressed in the normal masseter.

Animals↗
PubMed1989

Chromatographic separation of alkaline phosphatase from dental enamel.

Alkaline phosphatase (AP) was prepared from partly mineralized bovine enamel by extraction in phosphate buffer, centrifugation and various chromatographic techniques. Chromatofocusing showed that the enamel enzyme possessed five isoelectric points at the acid pH level ranging from pH 5.7 to pH 4.4. Three enzyme peaks were eluted using low pressure chromatography with a Bio-gel column. With a HPLC gel filtration column the separation of the enamel extract resulted in only one peak with AP activity. The fractions of this peak were used to produce an antibody against bovine AP.

Alkaline Phosphatase↗
PubMed1988

A comparison between activities for non-specific esterases and esterproteases.

Electrophoretic separation of non-specific esterases and esterproteases from kidney, lung, and liver have been carried out in polyacrylamide gels. By use of zone electrophoresis, isoelectric focusing, and 2-dimensional electrophoresis it was found that most of the esterprotease bands had the same localization in the gels as non-specific esterase bands. A number of esterase bands showed no activity towards the esterprotease substrates and a single kidney band possessed esterprotease activity only. Isozymes of the ES-6 and ES-9 zones showed sex dependent esterprotease reactions. In sections esterase activity was located to all parts of the proximal tubule. In male kidneys, esterprotease activity was present in the 2nd segment of the convoluted tubule which is not connected to glomeruli and in the descending part of the proximal tubule. In female kidney only the descending part of the proximal tubule showed esterprotease activity.

Alanine↗
PubMed1988

Antikeratin antibodies in routine diagnostic pathology. A comparison of 10 different commercial antikeratins.

Ten commercially available antikeratin antisera were tested immunohistochemically on fresh frozen and formalin-fixed paraffin-embedded tissue. Eight of the antisera were in addition tested on protein-immunoblottings. For six of the antisera a good correspondence was found between our immunoblots and data given by the manufacturers. Two monoclonal antisera did not react with keratin proteins. On immunohistochemical testing two of the antibodies showed qualitatively identical staining on both frozen and paraffin sections without background staining. Three of the antibodies reacted weakly or not at all on paraffin sections but gave acceptable staining on frozen sections. Three of the antibodies showed acceptable staining on paraffin sections, but background staining on frozen sections and one antibody gave the reverse staining pattern. For one of the antibodies it was impossible to obtain an acceptable staining due to high non-specific binding of the secondary antibody. None of the antikeratins were true panepithelial tumour markers as all of them failed to detect keratin in at least one of the epithelial tumours. However, a combination of two or three antikeratins (Hybritech AE1 + AE3, Becton Dickinson No 7650, DAKO A622) covered most or all epithelial tumours examined. It is concluded that commercially available antisera show great variability with respect to quality and reactivity indicating that the majority need further purification, characterization and testing on tissues before they are introduced on the commercial market.

Antibodies↗
PubMed1988

Esterase profile of human masseter muscle.

The esterase profile of fresh human masseter muscle was investigated by use of histochemistry and electrophoresis. The histochemical methods included reactions for alpha-naphthyl esterase, myofibrillar ATPase, reverse myofibrillar ATPase and succinic dehydrogenase. In frozen sections of the muscle the coloured reaction product for esterases was present both as a diffuse sarcoplasmic coloration and as distinct granules. The intensity of diffuse reaction was used to classify the muscle fibres as strongly, moderately and weakly reacting. The fibres with strong esterase activity belonged to Type I and iiC. iM and Type II A fibres showed a moderate esterase reaction and Type II B fibres had a low activity. The electrophoretic gels stained for esterase activity showed that the human masseter muscle possesses a slow migrating double band with high enzyme activity and a cascade of faster migrating isoenzymes. In isoelectric focused gels the major esterases showed isoelectric points around pH 5.

Esterases↗
PubMed1986

Studies on the actions of glutaraldehyde, formaldehyde, and mixtures of glutaraldehyde and formaldehyde on tissue proteins.

The effects of aldehyde fixation on tissue proteins was studied using SDS-polyacrylamide gel electrophoresis. Fixation with low concentrations of formaldehyde or glutaraldehyde had only a slight effect on the protein banding pattern. On the other hand, most of the original protein bands were absent after a short treatment with mixtures of formaldehyde and glutaraldehyde. Spectral absorption measurements showed a stronger absorption at both gamma = 280 nm and gamma = 235 nm with the glutaraldehyde-formaldehyde mixture than with glutaraldehyde alone.

Aldehydes↗
PubMed1986

Differentiation-dependent expression of keratins in human oral epithelia.

The polypeptide composition of epithelial keratins varies with the state of differentiation. The epithelia lining the human oral cavity show regional variations in their histology. In the present study, paired samples of nonkeratinized buccal epithelium and keratinized hard palate epithelium were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and by immunoblots with monoclonal antibodies AE1, AE2, and AE3, and results were correlated with immunofluorescence staining of tissue sections of the same samples. Keratins from hard palate (Mr 67K, 63-65K, 58K, 56.5K, 56K, 50K, 48K) and epidermis (Mr 67K, 63-65K, 58K, 56.5K, 50K) were similar to each other but distinctly different from those of buccal epithelium (major bands of Mr 52K and 59K, minor bands of 50K and 58K). The immunoblot analysis further indicated the similarity of hard palate and epidermal keratins, in contrast to those of buccal epithelium. Each oral tissue expressed keratins of the type I (AE1, acidic) subfamily and type II (AE3, basic) subfamily. In tissue sections, the predominant staining pattern for nonkeratinized buccal epithelium was: AE1, positive in the basal layer; AE2, negative; AE3, positive in all layers. In contrast, the staining pattern for keratinized palatal epithelium was: AE1 and AE2, positive in the suprabasal layers; AE3, positive in all layers. Strong suprabasal AE1 staining in palate may be related to the presence of the 48K keratin. Some buccal samples showed an alternate staining pattern of spotty suprabasal staining with AE1 and AE2 which was correlated with the expression of the 56.5K and 63-67K keratins, as well as filaggrin. These results suggest differentiation-specific expression of the keratins and show immunologically detectable variation in the apparently normal differentiation pattern of nonkeratinized buccal epithelium.

Antibodies, Monoclonal↗
PubMed1986

Keratin proteins in human oral mucosa.

We have examined the keratin proteins in normal human oral mucosa from 6 different regions including hard palate, buccal mucosa, tongue, gingiva and floor of the mouth. Urea-dithiothreitol extracts of EDTA separated epithelia were analysed by SDS-PAGE and immunoblotting. Eight samples from each region were investigated and showed very little individual variation in the keratin profile on Coomasie Blue-stained gels. The keratinizing hard palate and gingiva expressed identical patterns and resembled the pattern of epidermis from the flank region. The normally non-keratinizing buccal mucosa and the mucosa of the floor of the mouth expressed polypeptides distinctly different from those of the keratinizing epithelia and lacked the high molecular weight keratins. The dorsal surface of the tongue and the commissure region showed a pattern intermediate between keratinizing and non-keratinizing epithelia. The greater sensitivity of the immunoblotting technique revealed that the non-keratinizing epithelia synthesized one of the high molecular polypeptides and that the tongue produced all the bands found in keratinizing epithelia, but in very small quantities. There are, thus, distinct differences in the keratin expression of oral epithelia which are related to the pattern of keratinization assessed histologically.

Adult↗
PubMed1986

Streptococci and activities of sucrases and alpha-amylases in supragingival dental plaque and saliva in three caries activity groups.

Thirty-eight young adults participated in the study. They were divided in a caries-inactive group, a low caries activity group and a moderate to high caries activity group. Total cultivable bacteria, Streptococcus salivarius, and S. mutans in plaque and saliva were quantitated on TSA, MS, and MSB plates, respectively. Sucrase activity was determined by measuring reducing sugars in plaque and saliva after incubation with sucrose. alpha-Amylase activity was determined by Pharmacia Phadebas Amylase test. The data were analyzed with the non-parametric Mann-Whitney U test. The only significant difference was observed for plaque alpha-amylase activity between the caries-inactive group and the moderate-high caries activity group (P less than 0.05). The lack of differences concerning the other variables is discussed mainly on the basis of the multifactorial character of dental caries and the possible insufficiency of the applied methods.

Adult↗
PubMed1986

Effects of different extraction media on the electrophoretic pattern of proteins from partly mineralized bovine enamel.

Five different extraction solutions were used to isolate matrix proteins from immature bovine enamel, to evaluate the effect of this procedure on the pattern obtained after electrophoresis. By sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the dominating protein fraction in the ethylenediaminetetraacetic acid extract had a molecular weight of 67,000 daltons. The acetic acid and phosphate buffer extracts contained mostly low molecular weight proteins. Isoelectric focusing showed that most of the enamel proteins had isoelectric points below pH 7.0.

Acetates↗
PubMed1986

Influence of cations on enamel phosphatase activity.

ATP and 5-Br-4-Cl-indoxyl phosphate were used as substrates for spectrophotometric measurement of phosphatase activity in partly mineralized bovine enamel. MgCl2, CaCl2, NaCl, and KCl were used as moderators of the enzyme activities. It is concluded that at least two phosphatases, active at alkaline pH, are present in the immature enamel matrix.

Alkaline Phosphatase↗
PubMed1986

Biochemical characterization of alkaline phosphatase from partly mineralized bovine enamel.

Alkaline phosphatase (AP) from partly mineralized bovine enamel was studied. The enzyme resembles alkaline phosphatases in other calcifying tissues. The Km was 0.46 mM; the phosphatase was strongly inhibited by 1 mM Levamisol or EDTA and it showed the same sensitivity towards heating as bone alkaline phosphatase. The inactivation caused by phosphate ions was approximately about 30%. In a zymogram, five isozymes of enamel alkaline phosphatase can be recognized. In a SDS-polyacrylamide gel a single band showing enzyme activity was visualized. This enzyme has an apparent molecular weight of 140,000.

Alkaline Phosphatase↗
PubMed1985

Biochemical and histochemical studies on alkaline phosphatase in normal and dystrophic muscle.

In muscles from dystrophic mice the activity of alkaline phosphatase is 50-75% higher than in their control littermates. In the dystrophic animals all muscle fibres show strong enzyme activity. It is suggested that during dystrophy amounts of an already existing muscle alkaline phosphatase are produced rather than that a synthesis of a new isoenzyme should be initiated.

Alkaline Phosphatase↗
PubMed1985

Immunoblotting demonstration of antibodies to the organic matrix of developing bovine enamel.

Antiserum was raised against an acetic acid extract of partly mineralized bovine enamel. By use of immunoblotting it was shown that rabbit antibodies react with both high and low molecular weight proteins. Most but not all of the enamel proteins isolated by different extraction solutions were antigenic identical. The blotting time was found to be important when immunoblotting of enamel proteins is carried out.

Animals↗