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2.
Scientifica (Cairo) ; 2016: 5430164, 2016.
Artigo em Inglês | MEDLINE | ID: mdl-27840770

RESUMO

Background. Breastfeeding is the optimal method for achieving a normal growth and development of the baby. This study aimed to study mothers' perceptions and practices regarding breastfeeding in Mangalore, India. Methodology. A cross-sectional study of 188 mothers was conducted using a structured proforma. Results. Importance of breast feeding was known to most mothers. While initiation of breast feeding within one hour of birth was done by majority of mothers, few had discarded colostrum and adopted prelacteal feeding. Mothers opined that breast feeding is healthy for their babies (96.3%) and easier than infant feeding (79.8%), does not affect marital relationship (51%), and decreases family expenditure (61.1%). However, there were poor perceptions regarding the advantages of breast milk with respect to nutritive value, immune effect, and disease protection. Few respondents reported discontinuation of breastfeeding in previous child if the baby had fever/cold (6%) or diarrhea (18%) and vomiting (26%). There was a statistically significant association between mother's educational level and perceived importance of breastfeeding and also between the mode of delivery and initiation of breast feeding (p < 0.05). Conclusion. Importance of breast feeding was known to most mothers. Few perceptions related to breast milk and feeding along with myths and disbeliefs should be rectified by health education.

3.
Biochem Biophys Res Commun ; 314(1): 166-73, 2004 Jan 30.
Artigo em Inglês | MEDLINE | ID: mdl-14715261

RESUMO

The urea-induced unfolding of 'N' isomer (occurring at pH 7.0) and 'B' isomer (occurring at pH 9.0) of human serum albumin was studied by fluorescence and circular dichroism spectroscopic measurements. Urea-induced destabilization in different domains of both the isomers was monitored by using domain specific ligands, hemin (domain-I), chloroform, bilirubin (domain-II), and diazepam (domain-III). Urea-induced denaturation of N and B isomers of HSA showed a two-step, three-state transition with accumulation of intermediates around 4.8-5.2M and 3.0-3.4M urea concentrations, respectively. During first transition (0-4.8M urea for N isomer and 0-3.0M urea for B isomer) a continuous decrease in diazepam binding suggested major conformational changes in domain-III prior to intermediate formation. On the other hand, binding of hemin, a ligand for domain-IB and chloroform, whose binding site is located in domain-IIA remains unchanged up to 5.0M urea for N isomer and 3.0M urea for B isomer. Similarly, fluorescence intensity of Trp-214 that resides in domain-IIA remained unchanged up to the above-said urea concentrations and decreased thereafter. Absence of any decrease in hemin binding, chloroform binding, and Trp-214 fluorescence suggested the non-involvement of domain-IB and domain-IIA in intermediate formation. A significant increase in bilirubin binding prior to intermediate formation showed favorable conformational rearrangement in bilirubin binding cavity formed by loop 4 of domain-IB and loop 3 of domain-IIA. Further, a nearly complete abolishment of bilirubin binding to both isomers around 7.0M and 6.0M urea concentrations, respectively, indicated complete separation of domain-I from domain-II from each other. From these observations it can be concluded that N to B transition of human serum albumin shifted the intermediate formation towards lower urea concentration (3.0-3.4M urea for B isomer as against 4.8-5.2M urea for N isomer). Further both the intermediates were found to possess similar alpha-helical (approximately 39%) content and ligand binding properties.


Assuntos
Bilirrubina/química , Clorofórmio/química , Diazepam/química , Hemina/química , Albumina Sérica/química , Ureia/química , Sítios de Ligação , Humanos , Isomerismo , Ligação Proteica , Conformação Proteica , Desnaturação Proteica , Dobramento de Proteína , Isoformas de Proteínas/química , Estrutura Terciária de Proteína , Albumina Sérica/classificação , Relação Estrutura-Atividade
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