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1.
Mondo Ortod ; 15(6): 639-44, 1990.
Article in Italian | MEDLINE | ID: mdl-2074878

ABSTRACT

The biocompatibility of unprecious metal alloys, particularly those containing nickel, is controversial. Nickel is a known cancerous agent, and the main responsible of metal allergic reactions in human. Dentists must be aware about risks related to this material. It is mandatory carry out careful anamnesis about nickel hypersensitivity avoiding it in subject with known hypersensibility.


Subject(s)
Dental Alloys/adverse effects , Drug Hypersensitivity , Nickel/adverse effects , Dermatitis, Contact/etiology , Humans , Materials Testing , Mouth Mucosa/drug effects
2.
Mondo Ortod ; 15(2): 145-50, 1990.
Article in Italian | MEDLINE | ID: mdl-2205795

ABSTRACT

The Author's aims was to review the role of the lower third molars in delayed crowding of the jaw. A global agreement exists on the fact that lower molars should be considered only one between several factors able to cause malocclusion. Finally, the germectomy of the third molars has to be performed only in carefully selected patients after a comprehensive diagnostic evaluation of the single case.


Subject(s)
Malocclusion/etiology , Molar, Third , Tooth Germ/surgery , Humans , Mandible , Mesial Movement of Teeth , Tooth Eruption , Tooth Extraction
3.
Int J Biochem ; 22(6): 611-5, 1990.
Article in English | MEDLINE | ID: mdl-2143151

ABSTRACT

1. The kinetic characteristics of the ATP hydrolysis by membrane-bound and Triton X-100 solubilized mitochondrial ATPase, during the isoproterenol-induced cardiomyopathy, were investigated. 2. An increase in the inhibitory action of the oligomycin, a decrease in the affinity of the ATP binding sites and an increase of both activation energy and rate of thermal inactivation were observed for mitochondrial ATPase. 3. The possibility that the changes described are related to the modifications of the active configuration of mitochondrial ATPase, during the isoproterenol-induced cardiomyopathy, is discussed.


Subject(s)
Adenosine Triphosphatases/metabolism , Adenosine Triphosphate/metabolism , Cardiomyopathies/chemically induced , Isoproterenol/toxicity , Mitochondria, Heart/enzymology , Animals , Cardiomyopathies/enzymology , Cardiomyopathies/metabolism , Detergents/pharmacology , Hydrogen-Ion Concentration , Hydrolysis , Male , Mitochondria, Heart/drug effects , Mitochondria, Heart/metabolism , Octoxynol , Polyethylene Glycols/pharmacology , Rats , Rats, Inbred Strains
4.
Mondo Ortod ; 14(5): 609-14, 1989.
Article in Italian | MEDLINE | ID: mdl-2640946

ABSTRACT

In this paper, the Authors present epidemiology, ethiopatology, diagnosis and treatments elements of the impacted canines. Furthermore they describe the different surgical techniques needed for the exposure of these teeth.


Subject(s)
Cuspid/pathology , Tooth Movement Techniques , Tooth, Impacted/surgery , Cuspid/surgery , Humans , Maxilla , Tooth, Impacted/therapy
5.
Minerva Stomatol ; 38(4): 461-6, 1989 Apr.
Article in Italian | MEDLINE | ID: mdl-2659960

ABSTRACT

The high incidence of third molar extraction is related to their frequent pathology. The use of an uncomplicated and reliable diagnostic and therapeutic protocol therefore became extremely important. The protocol has to include careful selection and preparation as well as the appropriate choice of instruments and surgical techniques. This is even more important, considering the elective nature of the procedure and the local and more rarely, systemic complications that could develop.


Subject(s)
Molar, Third , Tooth Extraction/methods , Humans , Mandible , Tooth Extraction/instrumentation
6.
Cell Mol Biol ; 35(5): 503-10, 1989.
Article in English | MEDLINE | ID: mdl-2611837

ABSTRACT

Rat matrix-induced alkaline phosphatase is an enzyme which requires magnesium and zinc ions for its maximal activity. Two Zn(II) ions and one Mg(II) ion are bound to each subunit of native dimeric enzyme. The presence of magnesium ion (10-100 microM) or zinc ion (7-20 nM) alone is sufficient to stimulate apoenzyme activity. However maximal activity (264 U/mg) requires the presence of both ions. Binding of Zn(II) ions to the Mg(II) binding site causes a strong inhibition of the apoenzyme while the binding of Mg(II) on Zn(II) binding site is not sufficient to stimulate PNPPase activity of the apoenzyme. Binding of both ions to the enzyme molecule did not change the apparent dissociation constant for PNPP hydrolysis.


Subject(s)
Alkaline Phosphatase/metabolism , Bone Matrix/enzymology , Magnesium/pharmacology , Zinc/pharmacology , Animals , Rats
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