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N Collins

Publications and source records attributed to N Collins.

86 records · Page 5Linked to original sources

Anatomical distribution of sterols in oysters (Crassostrea gigas).

Oysters (Crassostrea gigas) contain at least 8 predominant sterols as determined by gas liquid chromatography and a modified Liebermann-Burchard reaction. These sterols and the average amount found in mg/100 are: C26-sterol (22-trans-24-norcholesta-5, 22-diene-3 beta-ol), 19.1; 22-dehydrocholesterol, 15.1; cholesterol, 46.8; brassicasterol, 27.2; delta 5,7-sterols (i.e., 7-dehydrocholesterol) 22.5; 24-methylenecholesterol 29.1; 24-ethylcholesta-5,22-diene-3 beta-ol, 1.2; and 24-ethylcholesta-5-en-3 beta-ol, 12.7. The distribution of these sterols appears uniform (r2 = 0.938) between 5 major organs of the oyster. The percent body mass vs percent total sterols in these 5 organs are: mantle 44.1--41.4; visceral mass 30.3--36.7; gills 13.2--11.7; adductor muscle 8.3--3.7; and labial palps 4.2--6.5. The possible sources of these sterols are discussed.

Animals↗

The localization of glycollate-pathway enzymes in Euglena.

Isolation of organelles from broken-cell suspensions of phototrophically grown Euglena gracilis Klebs was achieved by isopycnic centrifugation on sucrose gradients. 2. Equilibrium densities of 1.23g/cm3 for peroxisome-like particles, 1.22g/cm3 for mitochondria and 1.17g/cm3 for chloroplasts were recorded. 3. The enzymes glycollate dehydrogenase, glutamate-glyoxylate aminotransferase, serineglyoxylate aminotransferase, aspartate-alpha-oxoglutarate aminotransferase, hydroxy pyruvate reductase and malate dehydrogenase were present in peroxisome-like particles. 4. Unlike higher plants glycollate dehydrogenase and glutamate-glyoxylate aminotransferase were present in the mitochondria of Euglena. 5. Rates of glycollate and D-lactate oxidation were additive in the mitochondria, and, although glycollate dehydrogenase was inhibited by cyanide, D-lactate dehydrogenase activity was unaffected. 6. Glycollate oxidation was linked to O2 uptake in mitochondria but not in peroxisome-like particles. This glycollate-dependent O2 uptake was inhibited by antimycin A or cyanide. 7. The physiological significance of glycollate metabolism in Euglena mitochondria is discussed, with special reference to its role in photorespiration in algae.

Alcohol Oxidoreductases↗

Oxidative phosphorylation during glycollate metabolism in mitochondria from phototrophic Euglena gracilis.

Mitochondria were isolated by gradient centrifugation on linear sucrose gradients from broken cell suspensions of phototrophically grown Euglena gracilis. An antimycin A-sensitive but rotenone-insensitive glycollate-dependent oxygen uptake was demonstrated in isolated mitochondria. The partial reactions of glycollate-cytochrome c oxidoreductase and cytochrome c oxidase were demonstrated by using Euglena cytochrome c as exogenous electron acceptor/donor. Isolated mitochondria contain glycollate dehydrogenase and glyoxylate-glutamate aminotransferase and oxidize exogenous glycine. A P:O ratio of 1.7 was obtained for glycollate oxidation, consistent with glycollate electrons entering the Euglena respiratory chain at the flavoprotein level. The significance of these results is discussed in relation to photorespiration in algae.

Antimycin A↗

Microbody-marker Enzymes during Transition from Phototrophic to Organotrophic Growth in Euglena.

Transfer of Euglena gracilis Klebs Z cells from phototrophic to organotrophic growth on acetate results in derepression of the key enzymes of the glyoxylate cycle, malate synthase and isocitrate lyase, which appear coordinately regulated. The derepression of malate synthase and isocitrate lyase was accompanied by increased specific activities of succinate dehydrogenase, fumarase, and malate dehydrogenase, but hydroxypyruvate reductase activity was unaltered.Isolation of organelles from broken cell suspensions of cells grown heterotrophically on acetate was achieved by isopycnic centrifugation on sucrose gradients. Peaks of mitochondrial enzymes were obtained at equilibrium densities of 1.22 g cm(3) and 1.16 g cm(3), and although significant differences in the distribution of tricarboxylic acid cycle enzymes between these two peaks were not recorded adenosine triphosphatase activity was detected only in the less dense fraction (1.16 g cm(3)) showing this contained damaged mitochondria. The peak of particulate glyoxylate cycle enzymes was at an equilibrium density of 1.25 g cm(3), this being the same as that for glycolate pathway enzymes from phototrophic cells. Citrate synthase, isocitrate lyase, malate synthase, and malate dehydrogenase were all present in this fraction so it was concluded that Euglena glyoxysomes contain a complete glyoxylate cycle.

Journal Article↗

Peroxidative Activity in Euglena gracilis.

Cell-free homogenates of Euglena gracilis contain very low levels of catalase activity as compared to higher plants and some other algae. Purified Euglena cytochrome c acts catalytically as a peroxidase. The observed catalytic activity of cytochrome c in extracts from heterotrophically grown cells was more than enough to account for the observed rates of hydrogen peroxide destruction. The peroxidative activity of Euglena cytochrome c was completely inhibited by 20 mm 3-amino-1,2,4-triazole.

Journal Article↗

Identification of the breast cancer susceptibility gene BRCA2.

In Western Europe and the United States approximately 1 in 12 women develop breast cancer. A small proportion of breast cancer cases, in particular those arising at a young age, are attributable to a highly penetrant, autosomal dominant predisposition to the disease. The breast cancer susceptibility gene, BRCA2, was recently localized to chromosome 13q12-q13. Here we report the identification of a gene in which we have detected six different germline mutations in breast cancer families that are likely to be due to BRCA2. Each mutation causes serious disruption to the open reading frame of the transcriptional unit. The results indicate that this is the BRCA2 gene.

Amino Acid Sequence↗

Assessment and treatment of involuntary weight loss and protein-calorie malnutrition.

Involuntary weight loss and protein-calorie malnutrition have a great impact on the entire health care system, resulting in reduced quality of life for the affected patient, compromised recovery, and added financial costs to the institution where the patient is receiving care. In addition, regulatory agencies are placing increased emphasis on the timely assessment and treatment of involuntary weight loss and protein-calorie malnutrition. In this context, a multidisciplinary approach to prevention of weight loss and protein-calorie malnutrition offers the greatest opportunity for success. Early recognition of protein-calorie malnutrition using anthropometric data, laboratory findings, and physical examination with a comprehensive diet history is essential to timely and effective treatment. Treatment must be closely monitored by a nutrition professional and must proceed along the accepted continuum of interventions.

Cost of Illness↗