Histological and Biochemical Observations of Developing Enameloid of the Sea Bream

1987 ◽  
Vol 1 (2) ◽  
pp. 191-195 ◽  
Author(s):  
K. Kawasaki ◽  
S. Shimoda ◽  
M. Fukae
Keyword(s):  
Proteolytic Activity ◽  
Developmental Stages ◽  
Proteolytic Enzymes ◽  
Sea Bream ◽  
Total Protein Content ◽  
Noncollagenous Proteins ◽  
Saturated Atmosphere ◽  
Tooth Germs ◽  
Water Saturated ◽  
Cryostat Sections

In order to study changes in the enameloid matrix of the Sea Bream during the course of its development, we selected the developmental tooth germs of this fish as representative of three different developmental stages: "chalk-like", "cheese-like", and "soft" enameloid. The protein, calcium, and phosphate contents of each sample were analyzed. The changes of the total protein content in each sample suggest that a major part of the proteins decreased during maturation, although newly formed enameloid of the Sea Bream contains collagen and noncollagenous proteins. The existence of proteolytic activity was examined by placement of undemineralized cryostat sections of unfixed tooth germs on exposed and processed photographic films and then incubation for 30 min in a water-saturated atmosphere at 37°C. Proteolytic activity could be detected in the enameloid matrix, which appeared to be in a "cheese-like" stage. It is suggested that proteolytic enzymes play an important role in the removal of proteins during the maturation of enameloid, although the detailed mechanism of the process is still obscure.

scholarly journals Proteolytische Aktivität der lysosomalen Enzyme in der Leber wachsender Mäuse

2000 ◽  
Vol 43 (4) ◽  
pp. 363-374
Author(s):  
M. Schmidt ◽  
T. Król ◽  
U. Renne ◽  
L. Panicke
Keyword(s):  
Postnatal Development ◽  
Proteolytic Activity ◽  
Cathepsin D ◽  
Proteolytic Enzymes ◽  
Body Growth ◽  
Male Mice ◽  
High Body

Abstract. Title of the paper: Lysosomal proteolytic activity in the liver of growing mice The behaviour of the activity of some lysosomal proteolytic enzymes in Üie liver of mice, both selected and unselected for high body growth, was followed during the postnatal development. The activity of cathepsin D and L, the alanylaminopeptidase, the arginylaminopeptidase, the α-glucosidase and the N-acetyl-glucosaminidase was estimated in male mice aging 21, 28, 35 and 42 days. In the liver of animals with high body gain statistic significant lower activities (30–50 %) of all estimated enzymes were found, in comparison to the control mice. These results confirm the Statement mat inhibition of proteolysis is an immediate mechanism in the induction of growth.

scholarly journals SELECTED PROTEOLYTIC ACTIVITY BY EXTRACTS OF DERMESTID LARVAE

2011 ◽  
Vol 19 (19) ◽  
pp. 79-83
Author(s):  
Lavinel G. IONESCU
Keyword(s):  
Enzyme Activity ◽  
Ammonium Sulfate ◽  
Proteolytic Activity ◽  
Specific Activity ◽  
Proteolytic Enzymes ◽  
High Specific Activity ◽  
Water Extract ◽  
Dermestes Maculatus ◽  
Crude Preparation

The larvae of the Beetle Dermestes maculatus De Geer can subsist on a diet consisting largely of protein. Studies have been undertaken to investigate the nature of proteolytic enzymes. A water extract of the larvae yielded a crude preparation that hydrolyzes gelatin, bide powder, hemoglobin substrate, benzoyl-DL-arginine p-nitroamilide, and glutaryl-L-phenylalanine p-nitroanilide. Enzyme activity was found in a non-dialyzable, heat- and acid0labile portion of the extract yielded two fractions with high specific activity towards gelatin. These are precipitated between 40% to 60% saturation of ammonium sulfate and 60% to 80% saturation. The higher specific activity was observed in the 40%-60% fraction. These results suggest that the larvae of these dermestids contain proteolytic enzymes with actions similar to mammalian trypsin and chymotrypsin. The results also suggest that other proteolytic enzymes may be present as well.

scholarly journals Effect of Olive-Pine Bottom Ash on Properties of Geopolymers Based on Metakaolin

2019 ◽  
Author(s):  
Eduardo Bonet-Martínez ◽  
Pedro García-Cobo ◽  
Luis Pérez-Villarejo ◽  
Eulogio Castro ◽  
Dolores Eliche-Quesada
Keyword(s):  
Room Temperature ◽  
Bottom Ash ◽  
Raw Material ◽  
Climatic Chamber ◽  
General Terms ◽  
Saturated Atmosphere ◽  
Naoh Solution ◽  
Alkaline Activator ◽  
Water Saturated ◽  
Potential Use

In this research, the feasibility of using bottom ashes generated by the combustion of biomass (olive pruning and pine pruning) as a source of aluminosilicates (OPBA) has been studied, replacing the metakaolin precursor (MK) in different proportions (0, 25, 50, 75 and 100 wt. % substitution) for the synthesis of geopolymers. As alkaline activator an 8 M NaOH solution and a Na2SiO3 have been used. The geopolymers were cured 24 hours in a climatic chamber at 60 ° C in a water-saturated atmosphere, subsequently demoulded and cured at room temperature for 28 days. The results indicated that the incorporation of OPBA waste, which have 19.7 wt. % of Ca, modifies the characteristics of the products formed after alkaline activation. In general terms, the incorporation of increasing amounts of calcium-rich ashes results in geopolymers with higher bulk density. The compressive strength increases with the addition of up to 50 wt. % of OPBA with respect to the control geopolymers, contributing the composition of the residue to the acquisition of a better behaviour mechanical. The results indicate the potential use of these OPBA waste as raw material to produce unconventional cements with 28-day curing strengths greater than 10 MPa, and thermal conductivities less than 0.35 W/mK.

scholarly journals Expression, localization and synthesis of small leucine-rich proteoglycans in developing mouse molar tooth germ

2020 ◽  
Vol 64 (1) ◽  
Author(s):  
Angammana Randilini ◽  
Kaoru Fujikawa ◽  
Shunichi Shibata
Keyword(s):  
Organ Culture ◽  
Developmental Stages ◽  
Tooth Development ◽  
Expression Patterns ◽  
Tooth Germ ◽  
Molar Tooth ◽  
Cervical Region ◽  
Metabolic Labeling ◽  
Tooth Formation ◽  
Tooth Germs

The gene expression and protein synthesis of small leucine-rich proteoglycans (SLRPs), including decorin, biglycan, fibromodulin, and lumican, was analyzed in the context of the hypothesis that they are closely related to tooth formation. In situ hybridization, immunohistochemistry, and organ culture with metabolic labeling of [35S] were carried out in mouse first molar tooth germs of different developmental stages using ICR mice at embryonic day (E) 13.5 to postnatal day (P) 7.0. At the bud and cap stage, decorin mRNA was expressed only in the surrounding mesenchyme, but not within the tooth germ. Biglycan mRNA was then expressed in the condensing mesenchyme and the dental papilla of the tooth germ. At the apposition stage (late bell stage), both decorin and biglycan mRNA were expressed in odontoblasts, resulting in a switch of the pattern of expression within the different stages of odontoblast differentiation. Decorin mRNA was expressed earlier in newly differentiating odontoblasts than biglycan. With odontoblast maturation and dentin formation, decorin mRNA expression was diminished and localized to the newly differentiating odontoblasts at the cervical region. Simultaneously, biglycan mRNA took over and extended its expression throughout the new and mature odontoblasts. Both mRNAs were expressed in the dental pulp underlying the respective odontoblasts. At P7.0, both mRNAs were weakly expressed but maintained their spatial expression patterns. Immunostaining showed that biglycan was localized in the dental papillae and pulp. In addition, all four SLRPs showed clear immunostaining in predentin, although the expressions of fibromodulin and lumican mRNAs were not identified in the tooth germs examined. The organ culture data obtained supported the histological findings that biglycan is more predominant than decorin at the apposition stage. These results were used to identify biglycan as the principal molecule among the SLRPs investigated. Our findings indicate that decorin and biglycan show spatial and temporal differential expressions and play their own tissue-specific roles in tooth development.

A study on the degradation of arachin by proteolytic enzymes

1973 ◽  
Vol 51 (11) ◽  
pp. 2217-2222 ◽  
Author(s):  
R. B. van Huystee
Keyword(s):  
Amino Acids ◽  
Proteolytic Activity ◽  
Free Amino Acids ◽  
Free Amino ◽  
Proteolytic Enzymes ◽  
Disc Electrophoresis ◽  
Polyacrylamide Gels ◽  
Macromolecular Protein

The prime purpose of this proteolysis study was to direct attention to alternate means of measuring proteolytic activity other than the determination of free amino acids. The release of peptides from a macromolecular protein during incubation with either papain, pronase, or trypsin was determined by measuring the presence of 280-nm-absorbing molecules in the fractionation range of Sephadex G 25 eluant after incubation. The formation of larger proteinaceous constituents by proteolysis of arachin was analyzed by disc electrophoresis on polyacrylamide gels. Using these techniques it was noted that papain was the most efficient proteolytic agent for the degradation of arachin.

scholarly journals Effect of Olive-Pine Bottom Ash on Properties of Geopolymers Based on Metakaolin

Materials ◽  
2020 ◽  
Vol 13 (4) ◽  
pp. 901
Author(s):  
Eduardo Bonet-Martínez ◽  
Pedro García-Cobo ◽  
Luis Pérez-Villarejo ◽  
Eulogio Castro ◽  
Dolores Eliche-Quesada
Keyword(s):  
Room Temperature ◽  
Bottom Ash ◽  
Raw Material ◽  
Climatic Chamber ◽  
General Terms ◽  
Saturated Atmosphere ◽  
Naoh Solution ◽  
Alkaline Activator ◽  
Water Saturated ◽  
Potential Use

In this research, the feasibility of using bottom ashes generated by the combustion of biomass (olive pruning and pine pruning) as a source of aluminosilicates (OPBA) has been studied, replacing the metakaolin precursor (MK) in different proportions (0, 25, 50, 75, and 100 wt.% substitution) for the synthesis of geopolymers. As alkaline activator an 8 M NaOH solution and a Na2SiO3 have been used. The geopolymers were cured 24 h in a climatic chamber at 60 °C in a water-saturated atmosphere, subsequently demoulded and cured at room temperature for 28 days. The results indicated that the incorporation of OPBA waste, which have 19.7 wt.% of Ca, modifies the characteristics of the products formed after alkaline activation. In general terms, the incorporation of increasing amounts of calcium-rich ashes results in geopolymers with higher bulk density. The compressive strength increases with the addition of up to 50 wt.% of OPBA with respect to the control geopolymers, contributing the composition of the residue to the acquisition of better mechanical behavior. The results indicate the potential use of these OPBA waste as raw material to produce unconventional cements with 28-day curing strengths greater than 10 MPa, and thermal conductivities less than 0.35 W/mK.

Mise en évidence d'une production de protéases exocellulaires par les levures au cours de la fermentation alcoolique du moût de raisin

OENO One ◽  
1980 ◽  
Vol 14 (1) ◽  
pp. 37 ◽  
Author(s):  
Michel Feuillat ◽  
G. Brillant ◽  
J. Rochard ◽  
Chantal Hory
Keyword(s):  
Nitrogen Content ◽  
Proteolytic Activity ◽  
Alcoholic Fermentation ◽  
Proteolytic Enzymes ◽  
Malolactic Fermentation ◽  
Soluble Nitrogen ◽  
Proteolytic Stability ◽  
Short Time

<p style="text-align: justify;">La durée d'activité très limitée dans le temps des protéases du raisin est confirmée en vinification en blanc, mais une nouvelle activité protéolytique peut être caractérisée à 37 °C et à pH 3,7 dans le moût au cours de la fermentation alcoolique.</p><p style="text-align: justify;">Cette activité doit être attribuée à des protéases exocellulaires libérées dans le milieu des levures. Parmi les souches essayées <em>S. bayanus</em> a une activité protéolytique plus importante que <em>S. cerevisiae</em>, ce qui se traduit par l'obtention de vins plus riches en azote soluble, donc plus stables du point de vue protéique et vraisemblablement d'une meilleure fermentescibilité malolactique.</p><p style="text-align: justify;">+++</p><p style="text-align: justify;">The short time of activity of grape proteolytic enzymes is confirmed in fermentation off skins. However, a new proteolytic activity has been characterized at 37 °C and at pH 3.7, occuring in alcoholic fermentation of the must.</p><p style="text-align: justify;">This activity comes from exocellular proteolytic enzymes released by the yeasts in the medium. Among tested strains <em>S. bayanus</em> has a proteolytic activity greater than <em>S. cerevisiae</em>; so the soluble nitrogen content of wines is higher. According to this, proteolytic stability is better as, probably, malolactic fermentation capabilities.</p>

Some characteristics of extracellular proteases produced by members of the Chytridiales and the Spizellomycetales (Chytridiomycetes)

1994 ◽  
Vol 40 (2) ◽  
pp. 106-112 ◽  
Author(s):  
Thomas Krarup ◽  
Lauritz W. Olson ◽  
Hans Peter Heldt-Hansen
Keyword(s):  
Proteolytic Activity ◽  
Isoelectric Focusing ◽  
Serine Proteases ◽  
Proteolytic Enzymes ◽  
Complex Compounds ◽  
Extracellular Proteases ◽  
Peptide Substrates ◽  
Proteolytic Activities ◽  
Selection Of

The extracellular proteolytic enzymes of eight saprophytic, eucarpic, and monocentric isolates from two genera of the order Spizellomycetales and from one genus of the order Chytridiales (Chytridiomycetes) have been partially characterized. The isolectric points of the proteases were estimated from zymograms and demonstrate the existence of three types of proteolytic activity in most isolates. The proteases were tested against synthetic chromogenic peptide substrates and a selection of cations and more complex compounds, and the results suggest that parts of the extracellular proteolytic activities are due to proteases from two groups: the Ca2+ stabilized proteases and the alkaline serine proteases.Key words: serine proteases, metalloproteases, Chytridiomycetes, isoelectric focusing, chromogenic peptide substrates.

Growth and proteinase production inPseudomonasspp. cultivated under various conditions of temperature and nutrition

1968 ◽  
Vol 35 (3) ◽  
pp. 385-393 ◽  
Author(s):  
H. S. Juffs ◽  
A. C. Hayward ◽  
H. W. Doelle
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Proteolytic Activity ◽  
Proteolytic Enzyme ◽  
Organic Nitrogen ◽  
Proteolytic Enzymes ◽  
Dry Weight ◽  
Growth Cycle ◽  
Logarithmic Phase ◽  
Proteinase Production

SummaryA study was made of the formation of the extracellular proteolytic enzymes during the growth cycle of several species ofPseudomonascultivated under different conditions of temperature and nutrition. Proteolytic activity was not proportional to growth. Expressed per unit of cell dry weight, the proteolytic activity showed a peak in the early logarithmic phase which was greater in cultures grown at 3 than at 28°C. Proteolytic enzyme was not formed in the absence of organic nitrogen. Of 16 organisms studied,Pseudomonas aeruginosaATCC 10145 was the most prolific producer of proteolytic enzyme.

Enzymic Proteolysis byEntamoeba histolytica; biochemical characteristics and relationship with invasiveness

Parasitology ◽  
1960 ◽  
Vol 50 (3-4) ◽  
pp. 531-550 ◽  
Author(s):  
R. A. Neal
Keyword(s):  
Proteolytic Activity ◽  
Culture Media ◽  
Proteolytic Enzymes ◽  
Egg Yolk ◽  
Single Strain ◽  
High Proteolytic Activity ◽  
Serum Inhibitor ◽  
Sulphydryl Groups ◽  
Ph Range

The proteolytic activity of extracts ofEntamoeba histolyticahas been further investigated. Casein and gelatin, but not haemaglobin, were hydrolysed. Activity was observed in the pH range 5·8 to 8·5 with optimal activity at pH 7·5 to 7·9. Activity was optimal at 37° C. and sulphydryl groups were not required. Concomitant bacteria showed no proteolytic activity. Hyaluronidase, collagenase and lecithinase could not be detected.An inhibitor of proteolytic enzyme was present in sera of all animals tested and in egg yolk. All culture media prepared from eggs were inhibitory, but inspissation or dilution of serum inactivated the serum inhibitor. Purified trypsin inhibitors from lima and soy bean were not active against the amoebic enzyme. Proteolytic enzymes were not secreted extracellularlyin vitro.High proteolytic activity was found in two out of five invasive, freshly isolated, strains ofE. histolyticaand after two series of liver passages of a single strain. The significance of these observations is discussed. It is concluded that the present evidence does not convincingly demonstrate that high proteolytic activity is required for tissue invasion by amoebae, but may accompany another factor.

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