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1.
J Community Health Nurs ; 18(3): 139-50, 2001.
Article in English | MEDLINE | ID: mdl-11560107

ABSTRACT

The role of the home environment in the transmission of infectious diseases has been well described in the developing world but has received less attention in developed countries. An increasing focus on home hygiene has emerged in debates regarding the use of antimicrobial products in the home and the potential for development of resistance and in discussions regarding "when is clean too clean" and "what is clean." Studies are clearly needed to further explicate the role of the home in the spread of infectious agents, but before these can be conducted, adequate measurement tools are essential. This article describes extensive psychometric testing undertaken to develop valid and reliable methods and tools to measure home hygiene and focuses on a neighborhood that was primarily Spanish speaking in New York City. The Home Hygiene Assessment Tool described in this article can be used by clinicians and researchers to further elucidate the role of the home environment in the prevention and control of infections.


Subject(s)
Communicable Disease Control , Hygiene , Nursing Assessment/methods , Surveys and Questionnaires , Colony Count, Microbial , Health Behavior , Humans , New York City , Reproducibility of Results , Residence Characteristics
2.
Plant Physiol ; 110(3): 825-34, 1996 Mar.
Article in English | MEDLINE | ID: mdl-8819869

ABSTRACT

Lectins are carbohydrate-binding proteins that occur widely among plants. Lectins of plant vegetative tissues are less well characterized than those of seeds. Previously, a protein of soybean (Glycine max [L.] Merr.) leaves was shown to possess properties similar to the seed lectin. Here we show that the N-terminal amino acid sequence of this protein shares 63% identity with the seed lectin. Immunoblot analysis indicated that the protein occurs in leaves, petioles, stems, and cotyledons of seedlings but not in seeds. These observations prompted designation of the protein as a soybean vegetative lectin (SVL). Immunohistochemical localization in leaves indicated that SVL was localized to the vacuoles of bundle-sheath and paraveinal mesophyll cells. Removal of sink tissues or exposure to atmospheric methyl jasmonate caused increased levels of SVL in leaves and cotyledons. Co-precipitation of SVL and the soybean vegetative storage protein (VSP) during purification suggested an interaction between these proteins. SVL-horseradish peroxidase conjugate bound to dot blots of VSP or SVL, and binding was inhibited by porcine stomach mucin and heparin but not simple carbohydrates. Binding between SVL and VSP and similarities in localization and regulation support a possible in vivo interaction between these proteins.


Subject(s)
Glycine max/chemistry , Lectins/chemistry , Acetates/pharmacology , Amino Acid Sequence , Chromatography, Gel , Cyclopentanes/pharmacology , Immunoblotting , Immunohistochemistry , Lectins/isolation & purification , Lectins/metabolism , Molecular Sequence Data , Oxylipins , Plant Growth Regulators/pharmacology , Plant Leaves/chemistry , Plant Lectins , Protein Binding , Sequence Analysis , Glycine max/drug effects , Tissue Distribution
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