{"title":"[Juvenile delinquency].","authors":"U. Rimnon","doi":"10.4135/9781529714388.n371","DOIUrl":"https://doi.org/10.4135/9781529714388.n371","url":null,"abstract":"The growth of any civilization depends upon the children who are the yardsticks to measure its success. Children are the most vulnerable group in the society, and they are in need of greatest social care. The changes in the society have influenced the children to commit crime and through these changes the juveniles are heading towards the path of crime. Certain factors are responsible for the juveniles to commit delinquent acts such as the negative influence from peer groups and other socio-economic factors. Juvenile Delinquency is a deliberate issue as a delinquent child can become a persistent criminal in future. The Constitutional validity of laws [“Juvenile Justice (Care and Protection of Children) Act, 2015 replaced the Juvenile Justice (Care and Protection of Children) Act, 2000] relating to juvenile delinquency was challenged in the Supreme Court as it was against Article 14 .The involvement of juveniles in heinous crimes lead to the replacement of the old statute and categorized the children between the age of 16-18 years as an adult. This research paper deals with constitutional validity of laws relating to juvenile delinquency, Factors favoring juvenile delinquency and preventive measures.","PeriodicalId":7308,"journal":{"name":"Acta biochimica et biophysica; Academiae Scientiarum Hungaricae","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72786085","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Regulation of beta-adrenergic sensitivity by guanine nucleotides in rat brain.","authors":"M Wollemann","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Binding of beta-adrenergic receptor by labelled dihydroalprenolol was inhibited in the presence of GTP or GppNHp in rat brain particulate fractions. The inhibition was suspended when the particulate fraction was pretreated at 30 degrees C for 20 minutes and washed 3 times. It is concluded that the inhibition was due to endogenous bound catecholamines.</p>","PeriodicalId":7308,"journal":{"name":"Acta biochimica et biophysica; Academiae Scientiarum Hungaricae","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14152053","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Wandering of a black sheep.","authors":"V Csányi","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":7308,"journal":{"name":"Acta biochimica et biophysica; Academiae Scientiarum Hungaricae","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15029371","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
M Sasvári-Székely, M Staub, A Guttmann, V Törcsvári, F Antoni
{"title":"Pyrimidine salvage enzymes in human tonsil lymphocytes. I. Separation and properties of thymidine kinase isoenzymes.","authors":"M Sasvári-Székely, M Staub, A Guttmann, V Törcsvári, F Antoni","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Two forms of deoxythymidine kinase were separated from human tonsillar lymphocytes on DEAE-Sephadex column (peak 1 and peak 2 isoenzymes) and identified by gel electrophoresis. Both isoenzymes were found in freshly prepared lymphocytes as well as in lymphocytes cultured in the presence or absence of phytohaemagglutinin, but freshly prepared and phytohaemagglutinin-stimulated cells contained higher activity of peak 1 isoenzyme than the cultured, non-stimulated ones. Kinetic properties and feed-back inhibition of the two separated isoenzymes were compared. The apparent Km values of isoenzyme 1 and 2 were 4 microM and 5 microM for thymidine and were 0.15 mM and 0.12 mM for ATP, respectively. Isoenzyme 1 was found to be more sensitive to heat denaturation at 55 degrees C, and to feedback inhibition by dTTP than isoenzyme 2. On the contrary, isoenzyme 1 was more resistant to dCTP inhibition than the other one. It is concluded that the isoenzyme 1 activity correlates with the synthesis of DNA, while the activity of isoenzyme 2 seems to be constant. The high activity of isoenzyme 1 in freshly isolated tonsil lymphocytes supports their active proliferation in the organ.</p>","PeriodicalId":7308,"journal":{"name":"Acta biochimica et biophysica; Academiae Scientiarum Hungaricae","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14956299","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Is elastomucoproteinase a double-headed enzyme?","authors":"G Cs-Szabó, E Gyáni, I Banga, P Elödi","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>During isolation pancreatic elastase is accompanied by a minor component, elastomucoproteinase (EMPase), which can be separated in pure state by anion-exchange chromatography. EMPase exhibits both proteolytic and mucolytic activities. Applying powdered aortic preparations as a substrate, the enzyme can split off carbohydrate moieties, but it can also cleave peptide bonds as a proteinase. Assaying with tripeptide-p-nitroanilide substrates, the enzyme can decompose only those substrates which contain Phe or Tyr at the C-terminal. It appeared that the binding of Bz-Ala-Gly-Phe-pNA was the best, while the hydrolysis of Bz-Ala-Pro-Tyr-pNA was the fastest. Proteolytic activity of EMPase can be completely inhibited with phenylmethanesulphonyl fluoride, whereas its mucolytic activity only by 20%. The two activities may be located at two separate sites. The enzyme seemed to be composed of a single polypeptide chain by SDS-gel electrophoresis in the presence of urea and beta-mercapto-ethanol.</p>","PeriodicalId":7308,"journal":{"name":"Acta biochimica et biophysica; Academiae Scientiarum Hungaricae","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14079432","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Blood coagulation-fibrinolytic system and endothelial cells.","authors":"R Machovich","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Endothelial cells, under normal conditions, possess antithrombotic nature, whereas during damage, various components of the cell may initiate blood coagulation. These functions are greatly influenced and controlled by thrombin and plasmin through their direct actions or their formation in the blood coagulation-fibrinolytic system.</p>","PeriodicalId":7308,"journal":{"name":"Acta biochimica et biophysica; Academiae Scientiarum Hungaricae","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14152684","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Translational coupling at the intercistronic boundary of an artificially constructed operon in Escherichia coli.","authors":"G Szabó, P Venetianer","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>By using recombinant DNA techniques an artificial operon was constructed that codes for two fusion proteins under the control of the beta-lactamase promoter of plasmid pBR322. The two proteins are: 1. beta-lactamase-trp B (43 kd) 2. trpA-beta-galactosidase (120 kd). Frameshift mutations in the N-terminal region of the first gene resulted in a dramatic reduction in the synthesis of the protein coded by the second gene. This strong polar effect could not be accounted for by correspondingly lower level of the distal region of the messenger RNA, only by \"translational coupling\" due to the overlap of the termination codon of the first gene with the initiation codon of the second gene. It was concluded that the strong \"translational coupling\" observed in this artificial operon can be generally used to ensure coordinated high-level synthesis of proteins in operons constructed by recombinant DNA techniques.</p>","PeriodicalId":7308,"journal":{"name":"Acta biochimica et biophysica; Academiae Scientiarum Hungaricae","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15053201","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Stability, heat stability and heat sensitivity of proteins: thermodynamic considerations.","authors":"T Keleti","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The heat sensitivity and stability of a protein should be characterized by the Arrhenius parameters of the irreversible denaturation. The terms \"thermostability\" or \"activation enthalpy\" and \"activation entropy\" of denaturation as \"thermodynamic parameters of protein stability\" are misleading. The terms \"measure of heat sensitivity\" and \"measure of stability\" should be used as comparative data for protein structure.</p>","PeriodicalId":7308,"journal":{"name":"Acta biochimica et biophysica; Academiae Scientiarum Hungaricae","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14953702","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Abstracts. 13th meeting of the Hungarian Biophysical Society. 3-5 July, 1985, Debrecen.","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":7308,"journal":{"name":"Acta biochimica et biophysica; Academiae Scientiarum Hungaricae","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14951433","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
P I Bauer, Z Breuer, R Machovich, K G Büki, I Horváth
{"title":"Sensitivity of thrombin and plasmin to heparin and antithrombin III.","authors":"P I Bauer, Z Breuer, R Machovich, K G Büki, I Horváth","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Thrombin and plasmin are inactivated by antithrombin III at different rates. Heparin, at a catalytic amount, increases primarily the inactivation rate of thrombin. The two proteinases compete for heparin, i.e. heparin is preferably attached by thrombin. Furthermore, fibrinogen as well as fibrin protect plasmin against inactivation by antithrombin III. However, at high concentration of heparin, plasmin inactivation by antithrombin III is accelerated even in the presence of fibrinogen or fibrin.</p>","PeriodicalId":7308,"journal":{"name":"Acta biochimica et biophysica; Academiae Scientiarum Hungaricae","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14079435","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}