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1.
Crit Rev Microbiol ; 37(2): 141-56, 2011 May.
Article in English | MEDLINE | ID: mdl-21254832

ABSTRACT

Mycobacterium avium subsp. paratuberculosis (MAP) causes the disease of cattle, Johne's. The economic impact of this disease includes early culling of infected cattle, reduced milk yield, and weight loss of cattle sold for slaughter. There is a possible link between MAP and Crohn's disease, a human inflammatory bowel disease. MAP is also a potential human food borne pathogen because it survives current pasteurization treatments. We review the current knowledge of MAP, Johne's disease and Crohn's disease and note directions for future work with this organism including rapid and economical detection, effective management plans and preventative measures.


Subject(s)
Crohn Disease/microbiology , Mycobacterium avium subsp. paratuberculosis/isolation & purification , Paratuberculosis/microbiology , Animals , Cattle , Cattle Diseases/diagnosis , Cattle Diseases/drug therapy , Cattle Diseases/microbiology , Cattle Diseases/transmission , Crohn Disease/diagnosis , Crohn Disease/drug therapy , Humans , Mycobacterium avium subsp. paratuberculosis/genetics , Mycobacterium avium subsp. paratuberculosis/physiology , Paratuberculosis/diagnosis , Paratuberculosis/drug therapy , Paratuberculosis/transmission
2.
J Agric Food Chem ; 58(3): 1892-7, 2010 Feb 10.
Article in English | MEDLINE | ID: mdl-20052973

ABSTRACT

Protein fractions (water-soluble/albumin, salt-soluble/globulin, alkali-soluble/glutelin, and alcohol-soluble/prolamin) were extracted from defatted ripe bitter melon seed (Momordica charantia) using water, 1 M sodium chloride solution, alkali/pH 11.0, and 70% ethanol, sequentially. The main protein fraction was albumin (49.3%), followed by globulin (29.3%) and glutelin (3.1%). No prolamin was detected, and 18.3% of the protein was nonextractable. The surface hydrophobicities of albumin, globulin, and glutelin were 757, 1,034, and 292, respectively. The molecular sizes of all the fractions were mostly about 45 and 55 kDa. The denaturation temperatures of albumin, globulin, and glutelin were 111.9, 117.3, and 133.6 degrees C, respectively. The levels of all essential amino acids in the bitter melon protein fractions met the minimum requirements for preschool children (FAO/WHO/UNU) with the exception of Thr. Bitter melon protein fractions with unique protein profiles and higher denaturation temperatures could impart novel characteristics when used as food ingredients.


Subject(s)
Momordica charantia/chemistry , Plant Extracts/chemistry , Plant Extracts/isolation & purification , Plant Proteins/chemistry , Plant Proteins/isolation & purification , Chemical Fractionation , Globulins/chemistry , Globulins/isolation & purification , Glutens/chemistry , Glutens/isolation & purification , Hydrophobic and Hydrophilic Interactions , Molecular Weight , Protein Stability , Seeds/chemistry
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