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1.
Waste Manag ; 114: 331-340, 2020 Aug 01.
Article in English | MEDLINE | ID: mdl-32688065

ABSTRACT

Life Cycle Assessment (LCA) is a widespread tool used to guide decision-makers towards optimal strategic choices for sustainable growth. A key aspect of LCA studies of waste management systems where recycling activities are present is to account for resource recovery and the related substitution effects. Although multiple scientific papers assume a 1:1 substitution ratio between similar materials/products, this is often incorrect as the actual ratio is likely to vary. The focus of this paper is on the calculation of the substitutability coefficient for secondary materials based on technical characteristics. A state of the art literature review showed that many different calculation procedures were applied, which led to a wide variety of substitutability coefficients (sometimes provided under different terminology). In this perspective, the objective of this paper is to provide guidelines on the procedure to be followed to calculate the substitutability coefficient for secondary materials, based on technical characteristics. These guidelines are then applied to two waste management case studies, one dealing with bottom ashes from incineration and the other with plastic waste. In total, sixteen technical substitutability coefficients are given for ten secondary materials, based on state of the art and presented case studies. The paper thus represents a step forward in quantifying the substitutability of secondary materials in waste management LCA studies. The guidelines presented may allow other case studies to enrich the list of coefficients, useful for all LCA practitioners in a harmonized way allowing a more correct evaluation of the environmental impacts associated with recycling activities.


Subject(s)
Refuse Disposal , Waste Management , Environment , Incineration , Recycling
2.
Genomics ; 33(2): 199-206, 1996 Apr 15.
Article in English | MEDLINE | ID: mdl-8660968

ABSTRACT

A human gene encoding a putative RNA helicase, designated DDX10, was identified 400 kb telomeric to the ataxia-telangiectasia gene at chromosome 11q22-q23. The predicted amino acid sequence shows very high similarity to a subgroup of DEAD-box RNA helicases involved in ribosome biogenesis. This novel gene encodes a 3.2-kb transcript in a variety of human tissues. A processed pseudogene of DDX10 was detected at chromosome 9q21-q22. We observed a rare trinucleotide repeat length polymorphism within the coding sequence of DDX10.


Subject(s)
Chromosomes, Human, Pair 11 , RNA Nucleotidyltransferases/genetics , Amino Acid Sequence , Animals , Ataxia Telangiectasia/genetics , Base Sequence , Cell Line , Chromosomes, Human, Pair 9 , Cricetinae , DNA, Complementary , Gene Expression , Humans , Molecular Sequence Data , Pseudogenes , RNA Helicases , Sequence Homology, Amino Acid , Trinucleotide Repeats
3.
Hum Mol Genet ; 4(11): 2025-32, 1995 Nov.
Article in English | MEDLINE | ID: mdl-8589678

ABSTRACT

Ataxia-telangiectasia (A-T) is an autosomal recessive disorder involving cerebellar degeneration, immunodeficiency radiation sensitivity, and cancer predisposition. A-T heterozygotes are moderately cancer prone. The A-T gene, designated ATM, was recently identified in our laboratory by positional cloning, and a partial cDNA clone was found to encode a polypeptide with a PI-3 kinase domain. We report here the molecular cloning of a cDNA contig spanning the complete open reading frame of the ATM gene. The predicted protein of 3056 amino acids shows significant sequence similarities to several large proteins in yeast, Drosophila and mammals, all of which share the PI-3 kinase domain. Many of these proteins are involved in the detection of DNA damage and the control of cell cycle progression. Mutations in their genes confer a variety of phenotypes with features similar to those observed in human A-T cells. The complete sequence of the ATM gene product provides useful clues to the function of this protein, and furthers understanding of the pleiotropic nature of the A-T mutations.


Subject(s)
Protein Serine-Threonine Kinases , Proteins/genetics , Amino Acid Sequence , Animals , Ataxia Telangiectasia Mutated Proteins , Base Sequence , Cell Cycle , Cell Cycle Proteins/genetics , Cell Cycle Proteins/metabolism , Cloning, Molecular , DNA Repair , DNA-Binding Proteins , Humans , Molecular Sequence Data , Open Reading Frames , Phosphatidylinositol 3-Kinases , Phosphotransferases (Alcohol Group Acceptor)/genetics , Phosphotransferases (Alcohol Group Acceptor)/metabolism , Proteins/metabolism , Sequence Homology, Amino Acid , Tumor Suppressor Proteins
4.
Science ; 268(5218): 1749-53, 1995 Jun 23.
Article in English | MEDLINE | ID: mdl-7792600

ABSTRACT

A gene, ATM, that is mutated in the autosomal recessive disorder ataxia telangiectasia (AT) was identified by positional cloning on chromosome 11q22-23. AT is characterized by cerebellar degeneration, immunodeficiency, chromosomal instability, cancer predisposition, radiation sensitivity, and cell cycle abnormalities. The disease is genetically heterogeneous, with four complementation groups that have been suspected to represent different genes. ATM, which has a transcript of 12 kilobases, was found to be mutated in AT patients from all complementation groups, indicating that it is probably the sole gene responsible for this disorder. A partial ATM complementary DNA clone of 5.9 kilobases encoded a putative protein that is similar to several yeast and mammalian phosphatidylinositol-3' kinases that are involved in mitogenic signal transduction, meiotic recombination, and cell cycle control. The discovery of ATM should enhance understanding of AT and related syndromes and may allow the identification of AT heterozygotes, who are at increased risk of cancer.


Subject(s)
Ataxia Telangiectasia/genetics , Chromosomes, Human, Pair 11 , Phosphotransferases (Alcohol Group Acceptor)/genetics , Protein Serine-Threonine Kinases , Proteins/genetics , Amino Acid Sequence , Ataxia Telangiectasia Mutated Proteins , Cell Cycle , Cell Cycle Proteins , Chromosome Mapping , Chromosomes, Artificial, Yeast , Cloning, Molecular , DNA, Complementary/genetics , DNA-Binding Proteins , Female , Genetic Complementation Test , Genetic Predisposition to Disease , Heterozygote , Humans , Male , Meiosis , Molecular Sequence Data , Neoplasms/genetics , Nucleic Acid Hybridization , Phosphatidylinositol 3-Kinases , Phosphotransferases (Alcohol Group Acceptor)/chemistry , Phosphotransferases (Alcohol Group Acceptor)/physiology , Proteins/chemistry , Proteins/physiology , Radiation Tolerance , Sequence Deletion , Signal Transduction , Tumor Suppressor Proteins
5.
Biochem Mol Biol Int ; 33(3): 505-13, 1994 Jun.
Article in English | MEDLINE | ID: mdl-7524902

ABSTRACT

Polyclonal antibodies were produced against rat kidney gamma-glutamyl transpeptidase (GGT) and against a synthetic peptide corresponding to residues 512-534 in rat GGT. The anti-peptide antibody bound denatured GGT, acivicin-treated GGT and GGT absorbed to microtiter plates, but not GGT in solution, and did not inhibit GGT. The antibody against native GGT inhibited its activity in solution and did not bind efficiently adsorbed GGT in direct ELISA. It was active in direct and competition ELISA using kidney brush border membranes as the adsorbed antigen. The results indicate that these antibodies recognize conformational rather than sequence epitopes in GGT, and that marked changes occur in the conformation of GGT upon its absorption to plates or its reaction with acivicin.


Subject(s)
Antibodies/pharmacology , Kidney/enzymology , Peptide Fragments/immunology , gamma-Glutamyltransferase/chemistry , gamma-Glutamyltransferase/drug effects , Amino Acid Sequence , Animals , Binding Sites , Binding, Competitive , Enzyme-Linked Immunosorbent Assay , Epitopes/chemistry , Epitopes/immunology , Molecular Sequence Data , Protein Conformation , Rabbits , Rats , Structure-Activity Relationship , gamma-Glutamyltransferase/metabolism
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