Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 2 de 2
Filter
Add filters








Year range
1.
Invest. med. int ; 16(4): 235-9, feb. 1990. tab
Article in Spanish | LILACS | ID: lil-95540

ABSTRACT

Al considerara el grave problema estético y social que constituye la caspa, así como su elevada frecuencia entre la población, se decidió estudiar cuatro principios activos anticaspa, contra placebo. Se consideraron los parámetros clínicos más importantes: número de corneocitos, estudio micológico directo, cultivo, cutirreacción, prurito, irritación del cuero cabelludo y caida del cabello. Los resultados mostraron claramente que el disulfuro de selenio solo y en su presentación con acondicionador, fueron las sustancias más eficaces para combatir el problema


Subject(s)
Humans , Adolescent , Adult , Middle Aged , Male , Female , Dermatitis, Seborrheic/etiology , Dermatitis, Seborrheic/physiopathology , Dermatitis, Seborrheic/therapy , Disulfides/pharmacokinetics , Disulfides/therapeutic use , Selenium/pharmacokinetics , Selenium/therapeutic use
2.
An. acad. bras. ciênc ; 58(3): 355-62, 1986. tab
Article in English | LILACS | ID: lil-94852

ABSTRACT

The polymerization of hemoglobin Porto Alegre (HbPA) by inter-tetramer disulfide bond formation at pH 7.6 follows kinetics second order in Hb concnetration. The initial stage of the polymerization was associated with the formation of an HbPAS-S-S-HbPA octamer and a rate constant of 9 x 10***-2M***-1min***-1 was found at 13-C. A later stage of the polymerization wa associated with HbPA-S-S-HbPA-S-S-HbPA dodecamer formation and the rate constant calculated by an approximate treatment was found to be 2.8M***-1 at 13-C. The polymerization by intertetramer disulfide bond formation of HbPA in a 1:1 mixture with HbA follows second orfer kinetics and is monophasic. the lower rate constant found for the HbPA-S-S-HbA octamer (3.9 x 10***-2 M***-1min***-1 at 13-C) is attributed to the formation of S-S bond involving the thiols of the ß9 cysteine from HbPA and the ß93 cysteine from HbA. The 25.6 e.u. more positive "apparent" entropy of activation found for the dodecamer, when comapred to that of the HbPA-S-S-HbPA octamer, is interpreted as due to dehydration of electrically charged groups. The 15.6 e.u. more positive "apparent" entropy of activation of the HbPAS-S-HbA octamer when compared to that of the HbPA-S-S-HbPA octamer is also interpreted as due to dehydration


Subject(s)
Disulfides/pharmacokinetics , Hemoglobin A/metabolism , Edetic Acid , Philippines , Protein Conformation
SELECTION OF CITATIONS
SEARCH DETAIL