Cryptosporidiosis in the V Region Chile. III. Study of malnourished patients, 1985-1987

Frequency of infection by Cryptosporidium sp. in 1,039 faecal smears stained by Ziehl-Neelsen, obtained from undernourished patients of a Nutritional Recovery Center and an ambulatory undernourished center from the Fifth Region, Chile, were studied. All underwent a coproparasitological examination by the modified Telemann method. Thirty eight (3.7%) patients infected by the parasite were detected, with an overall frequency of 8.5% among patients of the Nutritional Recovery Center and 1.9% among the ambulatory patients; this difference was statistically significant. The highest percentage of positive results were detected among the younger milk feeding infants. Also the percentage of difference among these and the older milk feeding infants (3.7%) was statistically significant. Association of Cryptosporidium sp. and Giardia lamblia was observed in 6 ambulatory patients (2.3%).     

A computer analysis of electrophoresis and ultracentrifugation patterns.

A program DIANA is designed to fit the scanning curves of electrophoresis and ultracentrifugation patterns with 10-15 overlapping peaks by a sum of Gaussian-like distribitions. The parameters of the distributions are adjusted by minimizing x, using a problem oriented minimizing procedure. The number of molecular components as well as starting values of the positions and the widths of the peaks must be choosen as input for each type of pattern. Programs are written in FORTRAN IV.     

Structural studies on glycolipids. Part 1: 220 MHz pmr spectra of acetylated galactocerebrosides

The pmr spectra of fully acetylated 2S: 3R-2 amino-trans-4 octadecene-1, 3 diol (sphingosine) (lb), 2S : 3R-2 aminooctadecane-1, 3 diol (dihydrosphingosine) (2b), 1-O-β-D-galactopyranosyl-2S : 3R-2 tetracosanoylamido-trans-4 octadecene-1, 3 diol (cerasine) (3b), and 1-O-β-D-galactopyranosyl-2S : 3R-2 (2′ hydroxy) tetracosanoylamido-trans-4 octadecene-1, 3 diol (phrenosine) (4b), were determined in chloroform-d, acetone-d₆, and benzene-d₆ at 220 MHz. The relative chemical shifts of the various protons in the three solvents were different enough as to permit configurational and conformational information to be derived by partial first order analysis.     

Sensitivity of insect ovarian tissues to various pteridines as tested in tissue culture

The effect of pteridine derivatives and analogues on the cell outgrowth from the ovarian explants of the waxmoth, Galleria mellonella, was examined in hanging-drop cultures and cytochemical tests were made for succinate and glucose-6-phosphate dehydrogenases. Most of the derivatives and analogues of 2-amino-4-hydroxypteridine injured to a lesser or greater extent insect ovarian tissues in vitro, depending on the drug structure and the concentration applied. Of all the pteridine derivatives and analogues tested only 2-amino-4-mercaptopteridine and its C-6,7-dimethyl derivative (10 μM) promoted cell outgrowth from the explants as did folate.     

Bifunctional indole-3-acetyl transferase catalyses synthesis and hydrolysis of indole-3-acetyl-myo-inositol in immature endosperm of Zea mays

1- O -(indole-3-acetyl)- β - d -glucose: myo -inositol indoleacetyl transferase (IA- myo -inositol synthase) is an important enzyme in IAA metabolism. This enzyme catalyses the transfer of the indole acetyl (IA) moiety from 1- O -(indole-3-acetyl)- β - d -glucose to myo -inositol to form IA- myo- inositol and glucose. IA- myo -inositol synthase was purified to an electrophoretically homogenous state from maize liquid endosperm by fractionation with ammonium sulphate, anion-exchange, adsorption on hydroxylapatite, affinity chromatography on ConA-Sepharose, preparative PAGE and isoelectric focusing. We thus obtained two enzyme preparations which differ in their R _f on 8% polyacrylamide gel. The preparation of R _f 0.36 contained a single 56.4 kDa polypeptide, whereas the preparation of R _f 0.39 consisted of two polypeptides of 56.4 and 53.5 kDa. Both purified preparations of IAInos synthase also exhibited the activity of an IAInos hydrolase, showing that the dual activity was associated with a single protein. Results of gel filtration and analytical SDS-PAGE suggest that the native enzyme exists as both a monomeric (65 kDa) and homo- or heterodimeric form (110–130 kDa). Analysis of peptide maps and amino acid sequences of two 21 amino-acid peptides showed that polypeptides of 56.4 and 53.5 kDa have the same primary structure and that the 3 kDa difference in molecular mass is probably caused by different glycosylation levels. Comparison of this partial and internal amino acid sequence with sequences of other plant acyltransferases indicated similarity to several proteins which belonged to the serine carboxypeptidase-like (SCPL) acyltransferase family.