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1.
Rev. bras. enferm ; 67(6): 920-927, Nov-Dec/2014.
Article in Portuguese | LILACS, BDENF | ID: lil-732823

ABSTRACT

Este estudo objetivou compreender as práticas de cuidado dos profissionais de saúde que assistem os idosos Kaingang. Estudo qualitativo, apoiado na etnografia, realizado com dez profissionais à que atuam na atenção primária saúde da Terra Indígena Faxinal, Paraná, Brasil. Os dados foram coletados no período de novembro de 2010 a fevereiro de 2012 por meio da observação participante e entrevistas, e, analisados à luz da Teoria Transcultural do Cuidado. Identificaram-se como práticas de cuidado a medicação e imunização, bem como, cuidados da medicina tradicional. Para realização destes cuidados, os profissionais dispunham de estratégias que proporcionavam manutenção dos idosos na assistência. Conclui-se que valores culturais e científicos necessitam integrar a assistência para melhoria da saúde dos idosos indígenas.


This research aims to understand the care practices of health professionals who assist the elderly Kaingang. It is a qualitative study, supported in ethnography, conducted by ten professionals working in primary health care in the indigenous land of Faxinal, Paraná, Brazil. The data was collected from November 2010 to February 2012 by participant observation and interviews, and analyzed based on the Transcultural Care Theory. Was identified the preoccupation of the carers practices with the medication and immunization, as well as traditional medical care. To achieve these, care professionals had strategies that implemented maintenance of older people in care. We conclude that cultural values and integrate scientific need assistance to improve the health of elderly indigenous.


Este estudio tuvo como objetivo entender las prácticas de cuidado de los profesionales de la salud que asisten a los ancianos Kaingang. Estudio cualitativo, apoyado en la etnografía, llevado a cabo con diez profesionales que trabajan en la atención primaria de la salud de la tierra indígena de Faxinal, Paraná, Brasil. Los datos fueron recogidos a partir de noviembre 2010 a febrero 2012 a través de la observación participante y las entrevistas, y analizado con base en la Teoría del Cuidado Transcultural. Se identificaron las prácticas de atención médica y imunizacion,el cuidado de la medicina, así tradicional. Para lograrlo, los profesionales tenían estrategias que proporcionaban el mantenimiento de las personas mayores en su atención. Se concluye que los valores culturales y científicos necesitan ayuda para mejorar la salud de los ancianos indígenas.


Subject(s)
Animals , Rats , Liver/enzymology , Lysosomes/enzymology , Phospholipases A/metabolism , Phospholipases/metabolism , Protease Inhibitors/pharmacology , Cells, Cultured , Chymotrypsin/antagonists & inhibitors , Cysteine Proteinase Inhibitors/pharmacology , Leucine/analogs & derivatives , Leucine/pharmacology , Leupeptins/pharmacology , Oligopeptides/pharmacology , Pepstatins/pharmacology , Phospholipases A1 , Time Factors
2.
An. acad. bras. ciênc ; 81(3): 615-621, Sept. 2009. ilus, tab
Article in English | LILACS | ID: lil-523985

ABSTRACT

Obtained from leguminous seeds, various plant proteins inhibit animal proteinases, including human, and can be considered for the development of compounds with biological activity. Inhibitors from the Bowman-Birk and plant Kunitz-type family have been characterized by proteinase specificity, primary structure and reactive site. Our group mostly studies the genus Bauhinia, mainly the species bauhinioides, rufa, ungulata and variegata. In some species, more than one inhibitor was characterized, exhibiting different properties. Although proteins from this group share high structural similarity, they present differences in proteinase inhibition, explored in studies using diverse biological models.


Obtidas de sementes leguminosas, várias proteínas inibem proteinases de origem animal, incluindo humanas, e podem ser consideradas para o desenvolvimento de compostos com atividade biológica. Inibidores da família Bowman-Birk e da família Kunitz vegetal tem sido caracterizados em relação a especificidade para proteinase, estrutura primária e sitio reativo. O nosso grupo majoritariamente vem estudando o gênero Bauhinia, principalmente as espécies bauhinioides, rufa, ungulatae variegata. Em algumas espécies, mais de um inibidor com propriedades diferentes foi caracterizado. Embora tais proteínas apresentem alta similaridade estrutural, diferem quanto à inibição de proteinases, e foram exploradas em estudos utilizando diversos modelos biológicos.


Subject(s)
Animals , Humans , Fabaceae/chemistry , Protease Inhibitors/pharmacology , Chymotrypsin/antagonists & inhibitors , Fabaceae/classification , Peptides/isolation & purification , Peptides/pharmacology , Plant Proteins/isolation & purification , Plant Proteins/pharmacology , Plasma Kallikrein/antagonists & inhibitors , Protease Inhibitors/isolation & purification , Seeds/chemistry , Seeds/classification , Trypsin Inhibitor, Bowman-Birk Soybean/isolation & purification , Trypsin Inhibitor, Bowman-Birk Soybean/pharmacology
3.
Genet. mol. res. (Online) ; 6(4): 846-858, 2007. ilus, tab
Article in English | LILACS | ID: lil-520062

ABSTRACT

Bowman-Birk inhibitors (BBIs) are cysteine-rich and highly cross-linked small proteins that function as specific pseudosubstrates for digestive proteinases. They typically display a "double-headed" structure containing an independent proteinase-binding loop that can bind and inhibit trypsin, chymotrypsin and elastase. In the present study, we used computational biology to study the structural characteristics and dynamics of the inhibition mechanism of the small BBI loop expressing a 35-amino acid polypeptide (ChyTB2 inhibitor) which has coding region for the mutated chymotrypsin-inhibitory site of the soybean BBI. We found that in the BBI-trypsin inhibition complex, the most important interactions are salt bridges and hydrogen bonds, whereas in the BBI-chymotrypsin inhibition complex, the most important interactions are hydrophobic. At the same time, ChyTB2 mutant structure maintained the individual functional domain structure and excellent binding/inhibiting capacities for trypsin and chymotrypsin at the same time. These results were confirmed by enzyme-linked immunosorbend assay experiments. The results showed that modeling combined with molecular dynamics is an efficient method to describe, predict and then obtain new proteinase inhibitors. For such study, however, it is necessary to start from the sequence and structure of the mutant interacting relatively strongly with both trypsin and chymotrypsin for designing the small BBI-type inhibitor against proteinases.


Subject(s)
Animals , Endopeptidases/metabolism , Trypsin Inhibitor, Bowman-Birk Soybean/chemistry , Models, Molecular , Amino Acid Sequence , Cattle , Cluster Analysis , Drug Design , Trypsin Inhibitor, Bowman-Birk Soybean/pharmacology , Trypsin Inhibitors/chemistry , Chymotrypsin/antagonists & inhibitors
4.
Indian J Biochem Biophys ; 1991 Oct-Dec; 28(5-6): 418-24
Article in English | IMSEAR | ID: sea-26296

ABSTRACT

A protease inhibitor specific to trypsin and chymotrypsin was purified from horsegram (Dolichos biflorus) with the inhibition index 0.24 micrograms/micrograms for trypsin and 0.36 micrograms/micrograms for chymotrypsin. In SDS-PAGE, the inhibitor protein was seen as a single band with apparent molecular mass Mr = 15,500. However, on fast protein liquid chromatography (FPLC) or non-denaturating PAGE, the inhibitor resolved into four components revealing the existence of isoinhibitors. Data on amino acid analysis indicate that the isoinhibitors are closely related. The major amino acids in the inhibitor are half cystine (18.9 mole %), aspartic acid (12.7 mole %) and serine (14.3 mole %). The inhibitor was partially stable to 0.1% sodium dodecyl sulphate, 8M urea or 6M guanidine hydrochloride. The inhibitory activity was lost on reduction or carboxamidomethylation or acetylation. Modification of the arginine groups or CNBr cleavage of the protein did not result in significant loss of either tryptic or chymotryptic inhibitory activities. The isoinhibitors separated by FPLC reacted with polyclonal antibody raised in rabbits and had pI values ranging from 4.8-5.1. The horsegram inhibitor thus resembles other Bowman-Birk protease inhibitors.


Subject(s)
Amino Acids/analysis , Chymotrypsin/antagonists & inhibitors , Fabaceae/chemistry , Plants, Medicinal , Protease Inhibitors/chemistry , Trypsin Inhibitors/chemistry
6.
Southeast Asian J Trop Med Public Health ; 1983 Sep; 14(3): 349-52
Article in English | IMSEAR | ID: sea-34255

ABSTRACT

Serum protease inhibitors were determined in paired sera from 7 patients with cerebral malaria and 2 patients with acute malaria showing high and low growth inhibition activity in the initial and follow-up sera respectively. Alpha-1 antichymotrypsin and alpha-1 antitrypsin but not alpha-2 macroglobulin showed direct correlation with the growth inhibition activity. When alpha-1 antitrypsin was deliberately added to the malarial culture no growth inhibition occurred indicating that the alpha-1 antichymotrypsin was the most likely factor responsible for inhibition of growth of malarial parasites in vitro.


Subject(s)
Chymotrypsin/antagonists & inhibitors , Growth Inhibitors/metabolism , Humans , Malaria/blood , Plasmodium falciparum/metabolism , Protease Inhibitors/blood , alpha 1-Antichymotrypsin , alpha 1-Antitrypsin/blood , alpha-Macroglobulins/blood
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