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1.
J Biosoc Sci ; 53(3): 336-355, 2021 05.
Article in English | MEDLINE | ID: mdl-32326992

ABSTRACT

This study examined the effect of the Safe Adolescent Transition and Health Initiative (SATHI) programme on the use of maternal care services among rural, pregnant adolescents in India. This was an intensive community-based, multi-site intervention project conducted in Maharashtra state between 2008 and 2011. Its aims were to improve the reproductive health of married adolescent girls and avert the adverse consequences of early motherhood. It had a quasi-experimental, case-control, pre-post design to enable rigorous evaluation. This study used cross-sectional data from 644 married girls aged under 19 years at baseline and 802 at endline to assess the maternal care outcomes of antenatal care, delivery and postnatal services and nutrition during pregnancy. Difference-in-differences analysis showed that all outcomes improved significantly in the study sites between baseline and endline, and the improvement in study sites was significantly larger than in the control sites. Multivariate analysis showed a statistically significant dose-response effect of intervention participation for antenatal care, pregnancy nutrition and postnatal care. Study participation was not statistically significantly associated with higher rates of safe or institutional delivery. The analysis suggests that training and supporting community health workers to work with married adolescent girls using interpersonal communication and interacting frequently with them and their families and communities can significantly improve the use of maternal care services among this population. With almost a million community health workers and 200,000 auxiliary nurse midwives at the community level providing primary level care in India, this intervention offers a proven strategy to replicate and scale-up to reach large numbers of married adolescent girls who do not currently use maternal care services.


Subject(s)
Maternal Health Services , Adolescent , Aged , Cross-Sectional Studies , Female , Humans , India , Marriage , Pregnancy , Rural Population
2.
J Acquir Immune Defic Syndr ; 47(2): 248-52, 2008 Feb 01.
Article in English | MEDLINE | ID: mdl-18340657

ABSTRACT

INTRODUCTION: Sixty percent of India's HIV cases occur in rural residents. Despite government policy to expand antenatal HIV screening and prevention of maternal-to-child transmission (PMTCT), little is known about HIV testing among rural women during pregnancy. METHODS: Between January and March 2006, a cross-sectional sample of 400 recently pregnant women from rural Maharashtra was administered a questionnaire regarding HIV awareness, risk, and history of antenatal HIV testing. RESULTS: Thirteen women (3.3%) reported receiving antenatal HIV testing. Neither antenatal care utilization nor history of sexually transmitted infection (STI) symptoms influenced odds of receiving HIV testing. Women who did not receive HIV testing, compared with women who did, were 95% less likely to have received antenatal HIV counseling (odds ratio = 0.05, 95% confidence interval: 0.02 to 0.17) and 80% less aware of an existing HIV testing facility (odds ratio = 0.19, 95% confidence interval: 0.04 to 0.75). CONCLUSIONS: Despite measurable HIV prevalence, high antenatal care utilization, and STI symptom history, recently pregnant rural Indian women report low HIV testing. Barriers to HIV testing during pregnancy include lack of discussion by antenatal care providers and lack of awareness of existing testing services. Provider-initiated HIV counseling and testing during pregnancy would optimize HIV prevention for women throughout rural India.


Subject(s)
AIDS Serodiagnosis/statistics & numerical data , HIV Infections/diagnosis , Pregnancy Complications, Infectious/diagnosis , Adolescent , Adult , Cross-Sectional Studies , Female , Humans , India , Pregnancy , Rural Health , Surveys and Questionnaires
3.
J AOAC Int ; 88(4): 1142-7, 2005.
Article in English | MEDLINE | ID: mdl-16152933

ABSTRACT

A forced degradation study was successfully applied for the development of a stability-indicating assay method for determination of rosuvastatin Ca in the presence of its degradation products. The method was developed and optimized by analyzing the forcefully degraded samples. Degradation of the drug was done at various pH values. Moreover, the drug was degraded under oxidative, photolytic, and thermal stress conditions. Mass balance between assay values of degraded samples and generated impurities was found to be satisfactory. The proposed method was able to resolve all of the possible degradation products formed during the stress study. The developed method was successfully applied for an accelerated stability study of the tablet formulation. The major impurities generated during the accelerated stability study of the tablet formulation were matches with those of the forced degradation study. The developed method was validated for determination of rosuvastatin Ca, and the method was found to be equally applicable to study the impurities formed during routine and forced degradation of rosuvastatin Ca.


Subject(s)
Chromatography, Liquid/methods , Fluorobenzenes/analysis , Pyrimidines/analysis , Sulfonamides/analysis , Calcium/chemistry , Chromatography , Drug Stability , Hot Temperature , Hydrochloric Acid/analysis , Hydrogen-Ion Concentration , Hydroxymethylglutaryl-CoA Reductase Inhibitors/analysis , Light , Oxygen/analysis , Oxygen/chemistry , Placebos/analysis , Reproducibility of Results , Rosuvastatin Calcium , Sodium Hydroxide/analysis , Time Factors , Ultraviolet Rays
4.
J Parasitol ; 91(3): 585-90, 2005 Jun.
Article in English | MEDLINE | ID: mdl-16108551

ABSTRACT

The nucleotide sequence of a full-length cDNA encoding phosphofructokinase (PFK) enzyme from the parasitic nematode Ascaris suum was determined. The entire sequence of 2,653 bases comprises a single open reading frame of 2,452 bases and a noncoding region of 201 bases after the stop codon. The mature protein contains 812 amino acids and has a molecular mass of 90,900 Da. The amino acid sequences of several peptides derived from the purified protein show excellent correspondence with the translated nucleotide sequence. Comparison of the amino acid sequence of the protein with those of 3 other worms as well as those of human, rabbit, and bacterial enzymes reveals highly conserved regions interrupted with stretches of lesser sequence similarity. Analyses of the subunit primary structure reveal, as in other eukaryotic PFKs, that the amino-terminal half is homologous to the carboxy-terminal half, supporting the hypothesis that the PFK gene evolved by duplication of the prokaryotic gene and that the allosteric sites arose by mutations at the catalytic site. The location of the phosphorylation site is unique and different compared with other PFKs and plays a key role in regulation of the enzyme activity. Structural motifs such as the putative substrate and effector binding domains and also the key amino acids involved therein are clearly identified by alignment of all the PFK protein sequences.


Subject(s)
Ascaris suum/genetics , DNA, Helminth/chemistry , Phosphofructokinase-1/genetics , Amino Acid Sequence , Animals , Ascaris suum/enzymology , Base Sequence , Cloning, Molecular , Consensus Sequence , DNA, Complementary/chemistry , Humans , Mice , Molecular Sequence Data , Molecular Weight , Phosphofructokinase-1/chemistry , Rabbits , Sequence Alignment
5.
Protein Expr Purif ; 33(2): 209-13, 2004 Feb.
Article in English | MEDLINE | ID: mdl-14711508

ABSTRACT

The cDNA encoding fumarase, an enzyme catalyzing reversible hydration of fumarate to L-malate, from the parasitic roundworm Ascaris suum, has been cloned, sequenced, over-expressed in Escherichia coli, and purified. The single open reading frame translates into a protein of 50,502Da containing 467 amino acids. It shows 82, 77, and 58% identity with Caenorhabditis elegans, human, and E. coli fumC fumarases, respectively. The A. suum fumarase shows the signature sequence motif (GSSIMPGKVNPTQCE), which defines not only the class II fumarase family but also a much broader superfamily of proteins containing GSSxMPxKxNPxxxE motif. The coding region was cloned into pET101D-directional TOPO expression vector and transformed into E. coli BL21 Star (DE3). The protein after induction was expressed at high levels, almost 10% of the soluble protein, purified to near homogeneity, and appears identical to the enzyme purified from Ascaris suum.


Subject(s)
Ascaris suum/genetics , Cloning, Molecular , Fumarate Hydratase/genetics , Gene Expression , Amino Acid Sequence , Animals , Ascaris suum/enzymology , Base Sequence , Culture Media , Escherichia coli/genetics , Fumarate Hydratase/isolation & purification , Fumarate Hydratase/metabolism , Gene Library , Molecular Sequence Data , Molecular Weight , Recombinant Proteins/genetics , Recombinant Proteins/isolation & purification , Recombinant Proteins/metabolism , Sequence Homology, Amino Acid
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