Vaccination status of infants discharged from a neonatal intensive care unit.

OBJECTIVE: To determine the vaccination rate among infants discharged from a neonatal intensive care unit (NICU) and factors affecting that rate. DESIGN: Cross-sectional survey conducted when the children were 12 to 18 months of age. SETTING: NICU at the Royal University Hospital, Saskatoon, Sask. PARTICIPANTS: All 395 infants discharged from the NICU between Jan. 1 and June 30, 1992. MAIN OUTCOME MEASURES: Vaccination rate, ethnic background (native or non-native), place of residence (urban or rural), health status (number of days spent in the NICU), reasons for delay in or incomplete vaccinations (those involving parents'' responsibility, infant illness or contraindications). RESULTS: Of the 395 infants, 20 (5.0%) had died and incomplete information was available for 30 (7.6%). Complete data were available for 345 (87.3%). Of the infants for whom data were available, 8 (2.3%) had never been vaccinated and 142 (41.2%) had a delayed vaccination schedule or had not completed their scheduled vaccinations. Only 195 (56.6%) of the infants had received a full vaccination series. Non-native ethnic background was a predictor of completed vaccinations (odds ratio [OR] 5.40, 95% confidence interval [CI] 3.05 to 9.52). In a univariate model, urban area of residence was not a significant predictor of vaccination status, but when ethnic background was controlled for in a multivariate logistic regression analysis, urban area of residence was found to be inversely associated with completed vaccinations (OR 0.34, 95% CI 0.15 to 0.79). The number of days the child had spent in the NICU was not a significant predictor of vaccination status. CONCLUSION: The vaccination rate of infants discharged from the NICU is not optimal. Urban native children appears to be at risk of not being vaccinated. Non-native infants are five times more likely than native infants to have completed all of their scheduled vaccinations. Methods to improve the rate of completed vaccinations, especially for native children, must be sought and tested.     

A rapid method for the purification of D-amino acid oxidase of Trigonopsis variabilis by hydrophobic chromatography

Summary A relatively simple method has been described for the rapid purification of D-amino acid oxidase from Trigonopsis variabilis by hydrophobic chromatography on Phenyl-Sepharose CL-4B and negative adsorption on DEAE-cellulose. The purified enzyme had a specific activity of 22–24 units at 25°C and exhibited three bands on enzymatic staining.     

Diurnal rhythms of cortisol,ACTH, and beta-endorphin levels in neonates and adults.

To determine whether a diurnal rhythm exists in neonates admitted to neonatal intensive care units where there is continuous artificial lighting and periodic nursing and medical care, plasma cortisol, adrenocorticotropin (ACTH), and beta-endorphin concentrations were measured in two groups of infants and in adult human volunteers. As expected, a diurnal rhythm was seen in adults. A diurnal rhythm was also found for cortisol and endorphin levels in neonates (3 to 4 days postnatally) with minimal stress and in infants who were clinically severely stressed. There was not a significant difference between the morning and afternoon concentrations of ACTH in these infants, but the afternoon concentrations were lower than the morning''s, as would be expected. We found that a diurnal rhythm does exist in neonates within the first few days of postnatal life and that the continuous lighting and medical and nursing interventions do not interfere with this rhythm.     

Crystallization and preliminary data of Indian buffalo erythrocyte carbonic anhydrase

The most abundant anhydrase isoenzyme from the erythrocyte of Indian buffalo has been purified using affinity gel and DEAE-cellulose ion-exchange columns and single crystals suitable for X-ray diffraction studies have been obtained. The unit cell dimensions are a = 46.8 A, b = 104.5 A, c = 60.4 A, beta = 91.2 degrees and the space group is P2(1), with two molecules per asymmetric unit.     

Selective enhancement of the induction of alpha-lactalbumin activity in rat mammary explants by epidermal growth factor

Epidermal growth factor (EGF) enhances the induction of alpha-lactalbumin in mammary explants from pregnant and virgin rats in the presence of insulin (I), hydrocortisone (F) and prolactin (P). EGF also enhances the prolactin-independent induction of alpha-lactalbumin in tissue from pregnant rats and evokes prolactin-independent induction of alpha-lactalbumin in mammary tissue from virgin rats in the presence of I and F. Casein synthesis and galactosyltransferase activity are unaffected by EGF in the IFP-system, and are not induced in the IF-EGF-system. Multiplication stimulating activity, nerve growth factor, fibroblast growth factor and platelet-derived growth factor do not mimic the selective effects of EGF on rat alpha-lactalbumin. These influences of EGF on the differentiation of isolated rat mammary tissue are compared with those on mouse and rabbit tissue studied previously.     

Prostaglandin release by zygotes and endometria of pregnant rabbits

When 4-day rabbit zygotes were incubated for 1 h at 37 degrees C in vitro, very little prostaglandin (PG) was released into the medium, and the concentration of PGs in the zygotes after incubation was also low. The release of prostaglandin E (PGE) and prostaglandin F (PGF) into the medium, and their concentration in the zygotes after incubation, increased sharply on Days 6 and 7 of pregnancy, reaching, by Day 7, values close to 200 ng of each PG released in 1 h per mg of protein. By contrast, endometrial samples on Days 4 and 5 of pregnancy released more PGF and less PGE than the zygotes of the same ages on a per mg of protein basis, and on Days 6 and 7, less of both PGs. Furthermore, endometrial concentrations of PGs after incubation, except for PGF on Day 4, were always lower than values for zygotes. Endometrial concentrations of PGs on Day 6 were lower before than after incubation. Although there was a slight upward trend in PG release by endometrial samples with increasing length of pregnancy, the changes were minimal and, in the case of PGE, none of the mean values exceeded 1 ng per mg of protein. In 7-day blastocysts, high levels of both PGF and PGE were found in the blastocoelic fluid, and these did not change during the 1-h incubation. The release of PGF and PGE during in vitro incubation of ruptured and washed Day 6 blastocysts was stimulated by arachidonic acid, and that of PGF, but not PGE, inhibited by indomethacin. The release of PGE, but not of PGF, from Day 6 blastocysts was inhibited by low temperature, and the same conditions inhibited release of both PGF and PGE from endometrial cell suspensions. It seems that both blastocysts and endometria have capability to synthesize PGs, the blastocysts being particularly active in this regard on Days 6 and 7 of pregnancy. It is hypothesized that, in vivo, Day 6 and 7 blastocysts release large quantities of PGs which trigger some of the local endometrial changes associated with pregnancy.     

A unique and essential role for insulin in the phenotypic expression of rat mammary epithelial cells unrelated to its function in cell maintenance

Mammary explants from pregnant rats can be induced in regard to casein synthesis and alpha-lactalbumin activity when cultured in the presence of hydrocortisone, prolactin and levels of insulin approaching physiological concentrations. No detectable induction occurs in the absence of insulin. Although epidermal growth factor and multiplication stimulating activity, in the presence of hydrocortisone, can maintain the initial level of NADH-cytochrome c reductase as well as insulin, neither can substitute effectively for insulin in the induction of the milk proteins. Proinsulin, nerve growth factor, platelet-derived growth factor and fibroblast growth factor are also ineffective substitutes for insulin in this regard. Whereas prolonged tissue exposure to multiplication stimulating activity, hydrocortisone and prolactin does not result in induction of alpha-lactalbumin activity, subsequent addition of insulin leads to prompt response. The results suggest that the ability of insulin to function as a unique, essential factor in the induction of rat milk proteins is independent of its cell-maintenance activity. Thus, in addition to its well established functions in metabolic processes, insulin appears to play a vital role in certain developmental processes.     

Studies on the size and shape of rabbit intestinal glucoamylase-maltase complex.

Rabbit intestinal glucoamylase-maltase was examined in detail with respect to its molecular weight, sedimentation, diffusion and viscosity. It is a large asymmetrical molecule, with a molecular weight of 750 000-760 000. Its appearance under the electron microscope supports the idea that it is a long string (62.0 nm) consisting of eight beads of diameter 6.0 nm each and a surface-to-surface interbead distance of approx. 2.0 nm. The shape of the enzyme derived from its hydrodynamic behaviour by using the string-of-spherical-beads model originally proposed by Kuhn [(1932) Z. Phys. Chem. Abt. A 161, 1-32] and later modified by Shulman [(1953) J. Am. Chem. Soc. 75, 5846-5852] fits moderately well with the electron-microscopic picture. The beads might represent about six subunits, and the absence of sulphur from the enzyme and the inability to dissociate the enzyme by conventional methods indicate the possibility of unusual covalent cross-linking between the subunits and between the beads.     

Studies onGesonula punctifrons Stål (Orthoptera: Acrididae: Cyrtacanthacridinae) attacking water-hyacinth in India

Résumé L'AcridienGesonula punctifrons St?l attaque la Jacinthe d'eau (Eichhornia crassipes) dans plusieurs parties de l'Inde et est adapté à un habitat aquatique ou semi-aquatique. Les œufs, pondus dans les pétioles des feuilles, éclosent en 3 à 4 semaines. Les larves se développent en 4 à 5 semaines et demi, avec 5 mues. Les adultes vivent au maximum 4 à 5 mois en s'alimentant seulement de Jacinthe d'eau. En essais de laboratoire cet Acridien se nourrit activement deCanna orientalis dont les tiges sont percées de trous pour la ponte par les femelles, mais aucun œuf n'est déposé. Quarante trois autres plantes d'intérêt économique ont été expérimentées: plusieurs d'entre elles ont été l'objet d'attaques légères à modérées. L'analyse de la littérature concernant les plantes-h?tes du genreGesonula et la distribution deG. punctifrons montrent que cette espèce s'est adaptée secondairement àE. crassipes. Bien que cet Acridien s'observe en grand nombre dans quelques régions, l'ensemble de ses dégats à la mauvaise herbe n'est pas suffisant pour assurer le contr?le de celle-ci.

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This research has been financed in part by a grant made by the United States Department of Agriculture under P. L. 480.     

A simple quantitative assay for chloramphenicol acetyltransferase by direct extraction of the labeled product into scintillation cocktail.

A simple, rapid, sensitive, quantitative, and inexpensive assay for chloramphenicol acetyltransferase (CAT) is described. The assay is based on the direct extraction of the products of the reaction into toluene-based liquid scintillation cocktail. The assay is carried out in 7-ml scintillation vials using 1 mM chloramphenicol and either 100 microM acetyl-CoA and 0.1 microCi of [3H]acetyl-CoA or 1 mM acetyl-CoA and 0.5 microCi of [3H]acetyl-CoA. After incubation, the reaction is terminated with 0.5 ml of 0.1 M sodium borate-5 M NaC, pH 9. The acetylchloramphenicols are extracted with 5 ml of 0.4% 2,5-diphenyloxazole-0.005% 1,4-bis(5-phenyloxazol-2-yl)benzene in toluene by a 30-s shaking. After a short centrifugation to clarify the layers, the vials are counted in a liquid scintillation counter. Extracted products are stable in the organic layer. Under these conditions, nearly 100% extraction of acetylchloramphenicols is shown using nonlabeled compounds and spectrophotometric methods. Using pure enzyme in the assay, linearity of activity with enzyme concentration, time, and temperature of incubation is demonstrated. Assays may even be carried out at 60 degrees C, where the enzyme activity is 3.4-fold higher than that at 23 degrees C. The increase in enzyme activity with increasing temperature is due to the increased formation of predominantly 3-acetyl and 1-acetylchloramphenicols and not to 1,3-diacetylchloramphenicol. The present assay compared very well with the standard assay using [14C]chloramphenicol and TLC. Using this assay, we measured quantitatively the CAT activity in extracts of pSV2-CAT-transfected CV-1 cells in 10 min and NIH 3T3 cell extracts in 60 min at 60 degrees C.(ABSTRACT TRUNCATED AT 250 WORDS)