Assessment of Nutritional Status of Rural Tribal Children in Tripura.

This cross-sectional study evaluated the nutritional status of 608 rural tribal children (age 6 to 15 years) from Jampuijala block of West Tripura district, India. Prevalence of stunting, thinness and overweight were 23.7%, 33.4% and 0.8%, respectively. The prevalence of stunting and thinness was found to be higher in boys than in girls.

Nutritional Status of Tripuri Tribal Adolescent Boys of West Tripura District.

This cross-sectional study assesses the growth and nutritional status of 623 rural and urban Tripuri tribal adolescent boys (aged 8 to 15 years) from West Tripura district. Prevalence of stunting, thinness and overweight were observed 7.6%, 17.81% and 6.03% for urban and 27.9%, 38.37% and 0.39% respectively for rural boys.

Comparative studies on the interaction of protoporphyrin with hemoglobin and myoglobin.

The binding parameters of protoporphyrin IX (PPIX) with hemoglobin (Hb) were studied spectrofluorimetrically and the results were compared with those of PPIX interacting with myoglobin (Mb). Two concentration ranges of PPIX (0.3 microM-1.5 microM and 1.5 microM-3.0 microM) were used. For both hemoglobin and myoglobin, the binding affinity constant (K) decreased while the number of binding sites (p) increased as the concentration range of PPIX increased. The interactions occurred in non-cooperative mode. Over a particular PPIX range, the interaction of PPIX with hemoglobin decreased significantly with increasing NaCl molarity indicating a trend in electrostatic interaction, whereas PPIX binding with myoglobin did not change significantly indicating mostly non-electrostatic mode of interaction. Total bound charge (z psi) decreased significantly with increased PPIX concentration range in case of hemoglobin-PPIX interaction, but remained almost same in case of myoglobin-PPIX interactions. Thermodynamic analysis revealed that binding of PPIX to hemoglobin was mostly electrostatic at lower concentration range of PPIX but became less electrostatic at higher concentration range and myoglobin-PPIX interaction, predominantly hydrophobic in nature, became more hydrophobic with increased range of PPIX concentration. The difference in binding modality between PPIX-Hb and PPIX-Mb has been discussed in relation to the state of aggregation of porphyrin as well as the subunit interaction property present and absent in hemoglobin and myoglobin, respectively.