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1.
Indian J Psychiatry ; 46(3): 195-212, 2004 Jul.
Article in English | MEDLINE | ID: mdl-21224901

ABSTRACT

The information about Urban Mental Health Services has been nearly nonexistent in India, although the developed countries have been focusing on programmes for "Healthy Cities". The initiative taken as part of the WHO-ICMR Pilot Project on Urban Mental Health Services, with a public health perspective is being shared. The objectives of the Health Services Research (HSR) Arm of the project were to study the distribution and the availability of tertiary Mental Health Services, availability of human resources, average service load, mental health service gap, and perceptions of the users and the service providers, regarding the barriers in accessibility of mental health services, unmet service needs and strategies for improvement.The Research Methods involved Mapping Exercises with estimation of Service Loads and Qualitative Research Methods (QRM) like In-Depth Interviews (IDIs), Key Informant Interviews (KIIs), Free Listing and Focused Group Discussions (FGDs). The results indicate uneven availability of mental health services, human resource deficit specially for non-medical mental health professionals and mental health service gap (82% to96%). The average service load in the specialist mental health services is largely carried by the Govt. sector (half to two thirds), followed by the private sector (one third to half), with only a small portion by the NGO sector. The average mental health service load in the primary care general health services is largely carried by the private sector, with significant contribution from the non-formal service providers. The barriers to access, unmet needs and possible strategies as perceived by the community, users and service providers have been identified. The findings are discussed in the context of the mental health programmes and the public policy issues. The implications of the conclusions which suggest that Urban Mental Health Services are far from complete are highlighted.

2.
Ultrasound Obstet Gynecol ; 19(5): 475-7, 2002 May.
Article in English | MEDLINE | ID: mdl-11982981

ABSTRACT

OBJECTIVE: To compare pregnancy outcome after elective vs. ultrasound-indicated cervical cerclage in women at high risk of spontaneous mid-trimester loss or early preterm birth. METHODS: This was a retrospective study comparing two management strategies in women with singleton pregnancies who had at least one previous spontaneous delivery at 16-33 weeks of gestation. One group was managed by the placement of an elective cerclage at 12-16 weeks and the other group had transvaginal ultrasound examinations of the cervix at 12-15+6, 16-19+6, and 20-23+6 weeks and cervical cerclage was carried out if the cervical length was 25 mm or less. RESULTS: A total of 90 patients were examined, including 47 that were managed expectantly and 43 treated by elective cerclage. In the expectantly managed group, 59.6% (28/47) required a cervical cerclage. We excluded from further analysis three patients who were lost to follow-up and three because of fetal death or iatrogenic preterm delivery. Miscarriage or spontaneous delivery before 34 weeks' gestation occurred in 14.6% (6/41) of the elective cerclage group, compared with 20.9% (9/43) in the expectantly managed group (chi2 = 0.219, P = 0.640). CONCLUSION: In women at increased risk of spontaneous mid-trimester or early preterm delivery, a policy of sonographic surveillance followed by cervical cerclage in those with a short cervix reduces the need for surgical intervention without significantly increasing adverse pregnancy outcome.


Subject(s)
Cerclage, Cervical/methods , Obstetric Labor, Premature/prevention & control , Pregnancy Outcome , Pregnancy, High-Risk , Uterine Cervical Incompetence/diagnostic imaging , Uterine Cervical Incompetence/surgery , Chi-Square Distribution , Elective Surgical Procedures , Female , Gestational Age , Humans , Pregnancy , Retrospective Studies , Sensitivity and Specificity , Statistics, Nonparametric , Ultrasonography, Prenatal/methods
3.
Biochemistry ; 34(35): 11106-16, 1995 Sep 05.
Article in English | MEDLINE | ID: mdl-7669768

ABSTRACT

Resonance Raman (RR) spectra are reported for photosynthetic reactions centers (RCs) from the H(M200)L mutant of Rhodobacter capsulatus. In this mutant, the histidine residue which ligates the M-side bacteriochlorophyll (BCh) of the special pair primary donor (P) of wild-type RCs is replaced by a noncoordinating leucine. This results in the formation of a heterodimer primary donor (D) in which a bacteriopheophytin (BPh) replaces the M-side BCh. The RR data for the H(M200)L mutant were acquired at a large number of excitation wavelengths which span the B, Qx, and Qy absorption bands of the various bacteriochlorin cofactors in the RC. For comparison, spectra were also acquired for wild-type RCs at the same excitation wavelengths. The RR data obtained for the mutant indicate that heterodimer formation induces a variety of changes in the structural and electronic properties of the cofactors in the RC. These perturbations extend beyond the primary donor and include one of the two accessory BChs. Collectively, the RR studies indicate the following: (1) The structure of the single BCh cofactor in D [DL(BCh)] is different from that of either of the two BChs in P. However, DL(BCh) is more similar to PL than to PM. The PM cofactor is conformationally more distorted than either PL or DL(BCh). (2) The structure of the BPh cofactor in D [DM(BPh)] is similar to that of the other two BPhs in the RC. However, the frequency of the C9-keto carbonyl mode of DM(BPh) is anomalously low (1678 cm-1), as is also the case for PM. The vibrational characteristics of the C9-keto carbonyl vibrations of DM(BPh)/PM versus DL(BCh)/PL are consistent the notion that dielectric effects govern the frequency of the mode and that the effective dielectric constant is different on the L- versus M-sides of the primary donor. (3) Heterodimer formation perturbs the structural and electronic properties of one of the two accessory BChs (most likely BChL) in the RC. These perturbations are manifested as upshifts in the ring skeletal-mode frequencies and a blue-shift in the Qx absorption band (from 600 to 580 nm). The fact that heterodimer formation perturbs one of the accessory BChs suggests that global structural rearrangements occur in the protein matrix when the ligand to a cofactor in the primary donor is removed. (4) For both the H(M200)L mutant and wild-type RCs, oxidation of the primary donor significantly affects the RR cross section of the carotenoid.(ABSTRACT TRUNCATED AT 400 WORDS)


Subject(s)
Photosynthetic Reaction Center Complex Proteins/chemistry , Rhodobacter capsulatus/chemistry , Bacteriochlorophylls/chemistry , Bacteriochlorophylls/genetics , Carotenoids/chemistry , Electrochemistry , Light-Harvesting Protein Complexes , Molecular Structure , Oxidation-Reduction , Photosynthetic Reaction Center Complex Proteins/genetics , Point Mutation , Protein Conformation , Rhodobacter capsulatus/genetics , Spectrum Analysis, Raman
4.
Biochemistry ; 33(47): 14264-74, 1994 Nov 29.
Article in English | MEDLINE | ID: mdl-7947837

ABSTRACT

The pH dependence of the absorption and resonance Raman (RR) spectra of the deoxy and met forms of myoglobin (Mb) has been examined in detail. The spectral data were acquired at a number of different pHs (12) in the 2.6-7.6 range. RR spectra were obtained for both the low- and high-frequency regions by using a variety of excitation wavelengths ranging from the UV to the green. The data obtained for deoxyMb indicate that a spectroscopically distinct intermediate (I') exists at equilibrium in the pH 3.5-4.5 range. The I'-form of metMb could not be identified. The Soret absorption maximum of the I'-form of deoxyMb is at approximately 426 nm compared with the value of 435 observed for the native (N) form and 383 nm observed for the so-called unfolded (U') form which occurs in the pH 2.6-3.5 range. The absorption and vibrational spectra of the I'-form of deoxyMb observed at equilibrium are very similar to those of the intermediate that appears within a few milliseconds in pH-jump experiments. The RR data indicate that the structure of the heme group in the I'-form is distinctly different from that of either N- or U'-forms. The iron-histidine bond, characteristic of the N-form, is ruptured in both the I'- and U'-forms as is evidenced by the absence of the RR band due to the stretching vibration of this unit. In the I'-form, the histidine ligand is replaced by a relatively strongly bound, exchangeable water molecule. This ligand is absent in the U'-form. The aquo ligand of the five-coordinate heme in the I'-form is identified by a RR band at 411 cm-1 which undergoes a 15-17 cm-1 downshift in deuteriated buffer solutions. In contrast, none of the RR bands of the N- and U'-forms exhibit any significant isotope sensitivity. The properties of the I'-form and the conditions under which it is generated strongly suggest that this form corresponds to the molten globule intermediate of apoMb.


Subject(s)
Heme/chemistry , Myoglobin/chemistry , Deuterium , Hydrogen-Ion Concentration , Metmyoglobin/chemistry , Myoglobin/analogs & derivatives , Spectrophotometry , Spectrum Analysis, Raman
5.
J Biol Chem ; 269(19): 13966-78, 1994 May 13.
Article in English | MEDLINE | ID: mdl-8188677

ABSTRACT

Near-ultraviolet resonance Raman spectra of chloroperoxidase derivatives and high valent intermediates show frequencies that can be systematically assigned. In accord with previous observations of low v4 frequencies for the ferric enzyme, and quite low v4 frequencies for the ferrous enzyme, low v4 frequencies are observed for ferryl compound II and several ferric derivatives. Resonance Raman spectra of chloroperoxidase compound I feature upshifted v2, v11, and v37 frequencies and other characteristics that argue for a 2A1u in preference to a 2A2u ground state for the porphyrin phi-cation radical. A moderately intense anomalously polarized band is observed at a frequency typical for octaethylporphyrin phi-cation radicals, which have been previously assigned as the 2A1u radical type. Similar resonance Raman spectral attributes are observed for horseradish peroxidase compound I, supporting a 2A1u symmetry state assignment for this species also. A 2A1u symmetry state assignment for chloroperoxidase and horseradish peroxidase compounds I is consistent with the beta-pyrrole substituent pattern of the protoporphyrin hemes found in these enzymes.


Subject(s)
Chloride Peroxidase/chemistry , Mitosporic Fungi/enzymology , Catalysis , Chloride Peroxidase/metabolism , Oxidation-Reduction , Spectrum Analysis, Raman
6.
Biochemistry ; 31(45): 11050-8, 1992 Nov 17.
Article in English | MEDLINE | ID: mdl-1445843

ABSTRACT

Qy-excitation resonance Raman (RR) spectra are reported for reaction centers (RCs) from Rhodobacter sphaeroides 2.4.1. The RR spectra were acquired for both chemically reduced and oxidized RCs at 25 and 201 K by using a variety of excitation wavelengths in the range 800-920 nm. This range spans the Qy absorption bands of the special pair (P) and the accessory bacteriochlorophylls (BChls). The RR studies indicate that both P and the accessory BChls exhibit rich RR spectra in the 30-1800-cm-1 region. For both types of pigments, at least 20 bands are observed in the 30-750-cm-1 range. Although the frequencies of the modes of P and the accessory BChls are different, it is possible to make one-to-one correlations of the bands observed for the two types of pigments. This result suggests that the vibronically active low-frequency modes of P are derived from monomer-like vibrations (although they may be coupled monomer-like modes) rather than being vibrations resulting from the additional degrees of freedom present in the dimer. A plausible set of vibrational assignments for the low-frequency modes of both P and the accessory BChls is proposed on the basis of a semiempirical normal coordinate calculation. Comparison of the RR intensities of the low-frequency modes of P with those of the analogous modes of the accessory BChls indicates that the intensities of the modes of the former pigments are considerably larger than those of the latter. Collectively, the spectral data indicate that a large number of low-frequency modes of P are strongly coupled to the Qy electronic transition.(ABSTRACT TRUNCATED AT 250 WORDS)


Subject(s)
Photosynthetic Reaction Center Complex Proteins/chemistry , Rhodobacter sphaeroides/chemistry , Oxidation-Reduction , Spectrum Analysis, Raman , Temperature
7.
J Biol Chem ; 264(27): 16046-53, 1989 Sep 25.
Article in English | MEDLINE | ID: mdl-2777776

ABSTRACT

Resonance Raman enhancement of derivatives and intermediates of horseradish peroxidase in the near ultraviolet (N-band excitation) results in intensity and enhancement patterns that are different from those normally observed within the porphyrin Soret (B-band) and alpha-beta (Q-band) absorptions. In particular it allows the resolution of resonance Raman spectra of horseradish peroxidase compound I. The bands above 1300 cm-1 can be assigned to porphyrin vibrational modes that are characteristically shifted in frequency due to removal of an electron from the porphyrin ring. The resonance Raman frequency shifts follow normal mode compositions. Relative to resonance Raman spectra of compound II, the v4 frequency (primarily Ca-N) exhibits a 20 cm-1 downshift. The v2, v11, and v37 vibrational frequencies whose mode compositions are primarily porphyrin Cb-Cb, exhibit 10-20 cm-1 upshifts. The v3, v10, and v28 frequencies, whose mode compositions are primarily Ca-Cm, exhibit downshifts. The downshifts for v3 and v10 are small, 3-5 cm-1; however, the downshift for v28 is 14 cm-1. These frequency shifts are consistent with those of previously published resonance Raman studies of model compounds. In contrast to reports from other laboratories, the data presented here for horseradish peroxidase compound I can be attributed unambiguously to resonance Raman scattering from a porphyrin pi-cation radical.


Subject(s)
Horseradish Peroxidase/metabolism , Peroxidases/metabolism , Heme/analysis , Porphyrins/analysis , Protein Conformation , Spectrum Analysis, Raman , Ultraviolet Rays
8.
Indian J Psychiatry ; 25(4): 286-92, 1983 Oct.
Article in English | MEDLINE | ID: mdl-21847305

ABSTRACT

This report is based on the study of 40 depressives in an attempt to explore the possible association between the suicidal ideas and the biogenic amines. The severity of suicidal ideas was measured on Hamilton Depressive Rating Scale and their amine metabolites were measured (MHFG, HVA and 5 HIAA) in urine and C.S.F. It was observed that the level of 5 HIAA, and Serotonin (5 HT) was more related to suicidal ideas and was inversely related. The probable associations between these are discussed.

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