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7 Scientific Studies of Protein Synthesis and Raw Food

       
Results for your query On December 9, 2000:
Search all fields for: protein synthesis And raw food
Published in 1966 through 1999
Only select references with abstracts available
Show references published in English only

Documents: 1 to 7 of 7

1

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Bryan PJ, et al; Adaptive response to cold temperatures in Vibrio vulnificus. (Curr Microbiol, 1999 Mar, Abstract available) [MEDLINE]

2 Oliveira AC, et al; Type I collagen synthesis by rats fed beans (Phaseolus vulgaris, L.) as the protein source. (Braz J Med Biol Res, 1992, Abstract available) [MEDLINE]
3 Goena M, et al; Effect of the raw legume Vicia ervilia on muscle and liver protein metabolism in growing rats. (Rev Esp Fisiol, 1989, Abstract available) [MEDLINE]
4 Goena M, et al; Muscle and liver protein synthesis and degradation in growing rats fed a raw field bean (Vicia faba L.) diet. (Rev Esp Fisiol, 1988 Dec, Abstract available) [MEDLINE]
5 Martínez JA, et al; Nutritional outcome and immunocompetence in mice fed on a diet containing raw field beans (Vicia faba, var. minor) as the source of protein. (Br J Nutr, 1992 Sep, Abstract available) [MEDLINE]
6 Martínez JA, et al; Response of muscle, liver and whole-body protein turnover to two different sources of protein in growing rats. (Ann Nutr Metab, 1987, Abstract available) [MEDLINE]
7 Simat TJ, et al; Synthesis, formation, and occurrence of contaminants in biotechnologically manufactured L-tryptophan. (Adv Exp Med Biol, 1999, Abstract available) [MEDLINE]


       

Record 1 from database: MEDLINE
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Title
Adaptive response to cold temperatures in Vibrio vulnificus.
Author
Bryan PJ; Steffan RJ; DePaola A; Foster JW; Bej AK
Address
Department of Biology, University of Alabama at Birmingham, 1300 University Boulevard, Birmingham, AL 35294-1170, USA.
Source
Curr Microbiol, 1999 Mar, 38:3, 168-75
Abstract
The effectiveness of rapid chilling or freezing of oysters to reduce Vibrio vulnificus levels in shellfish may be compromised by product handling procedures that permit cold adaptation. When a V. vulnificus culture was shifted from 35 degrees C to 6 degrees C conditions, it underwent transition to a non-culturable state. Cells adapted to 15 degrees C prior to change to 6 degrees C condition, however, remain viable and culturable. In addition, cultures adapted to 15 degrees C were able to survive better upon freezing at -78 degrees C compared with cultures frozen directly from 35 degrees C. Inhibition of protein synthesis by addition of chloramphenicol in a V. vulnificus culture immediately prior to the exposure to the adaptive temperature eliminated inducible cold tolerance. These results suggest that cold-adaptive "protective" proteins may enhance survival and tolerance at cold temperatures. In addition, removal of iron from the growth medium by adding 2,2'-Dipyridyl prior to cold adaptation decreased the viability by approximately 2 logarithm levels. This suggests that iron plays an important role in adaptation at cold temperatures. Analysis of total cellular proteins on an SDS polyacrylamide gel electrophoresis, labeled with 35S-methionine during exposure at 15 degrees C, showed elevated expressions of a 6-kDa and a 40-kDa protein and decreased expression of an 80-kDa protein. These results suggest that, for V. vulnificus, survival and tolerance at cold temperatures could be due to the expression of cold-adaptive proteins other than previously documented major cold shock proteins such as CS7.4 and CsdA. In this study, for the first time we have shown that exposure to an intermediate cold temperature (15 degrees C) causes a cold adaptive response, helping this pathogen remain in culturable state when exposed to a much colder temperature (6 degrees C). This adaptive nature to cold temperatures could be important for shellfish industry efforts to reduce the risk of V. vulnificus infection from consuming raw oysters.
Language of Publication
English
Unique Identifier
99122924

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MeSH Heading (Major)
Adaptation, Physiological|*PH; Vibrio|CY/DE/GD/*PH
MeSH Heading
Animal; Antibiotics|PD; Autoradiography|MT; Bacterial Proteins|AN; Chloramphenicol|PD; Cold; Colony Count, Microbial; Comparative Study; Culture Media|CH; Food Microbiology; Heat-Shock Proteins|AN; Human; Oysters|MI; Refrigeration; Support, Non-U.S. Gov't; Support, U.S. Gov't, Non-P.H.S.; Time Factors

Publication Type
JOURNAL ARTICLE
ISSN
0343-8651
Country of Publication
UNITED STATES

Record 2 from database: MEDLINE
Return To Top

Title
Type I collagen synthesis by rats fed beans (Phaseolus vulgaris, L.) as the protein source.
Author
Oliveira AC; Vidal BC
Address
Departamento de Planejamento Alimentar e NutriÀcÃao, Faculdade de Engenharia de Alimentos, Universidade Estadual de Campinas, SP, Brasil.
Source
Braz J Med Biol Res, 1992, 25:5, 499-501
Abstract
Type I collagen synthesis was studied in 12 female Wistar rats weighing 60 +/- 5 g at the beginning of the experiment. The animals were fasted for 24 h and then injected ip with 10 microCi uniformly labeled [14C]-glycine. Two hours later, groups of 4 animals each were fed balanced diets (10.7 +/- 0.4% protein) containing raw beans (Phaseolus vulgaris, L.), cooked beans or casein (control) as the single protein source, ad libitum. The animals were killed after 4 days and collagen was extracted from the tail and calcaneal tendons. Food intake and weight gain of rats fed raw beans (22 g, 0 g) were considerably less than rats fed cooked beans (38 g, 9 g) and casein (44 g, 22 g). Collagen was quantitated on the basis of hydroxyproline and corresponded to 0.1, 0.2 and 0.2% rat body weight, with specific radioactivity of 1.2, 1.6 and 4.2 microCi/g, for the rats fed raw beans, cooked beans and casein, respectively. The results indicate that rats fed either bean protein synthesized less collagen than those fed casein (P < 0.05). Although the food intake and extractable collagen of rats fed cooked beans were similar to those of casein-fed rats, weight gain and collagen specific radioactivity were less.
Language of Publication
English
Unique Identifier
94100895

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MeSH Heading (Major)
Collagen|AN/*BI; Dietary Proteins|*AD; Legumes|*
MeSH Heading
Animal; Carbon Radioisotopes; Caseins|AD; Comparative Study; Cookery; Female; Rats; Rats, Wistar; Tail|CH; Tendons|CH

Publication Type
JOURNAL ARTICLE
ISSN
0100-879X
Country of Publication
BRAZIL

Record 3 from database: MEDLINE
Return To Top

Title
Effect of the raw legume Vicia ervilia on muscle and liver protein metabolism in growing rats.
Author
Goena M; Marzo F; Fernández González AL; Tosar A; Frühbeck G; Santidrián S
Address
Departamento de FisiologÆia, Facultad de Medicina, Universidad de Navarra, Pamplona, Spain.
Source
Rev Esp Fisiol, 1989, 45 Suppl:, 55-9
Abstract
Body weight gain (BWG), food intake, food efficiency rate (FER: food intake, g/protein intake, g), gastrocnemius muscle and liver weights, protein, RNA and DNA contents of gastrocnemius muscle and liver have been measured in growing rats (80-90 g initial body weight) fed ad libitum over a period of 11 days on 12.00% protein diets containing either heated and defatted Glycinae sojae (HSB) as control or the raw legume Vicia ervilia as the main sources of protein. It has been found that, as compared to HSB-fed rats, those fed the legume Vicia ervilia diet exhibited a significant reduction in growth, PER, FER, as well as, in RNA-activity (protein, g/day/RNA, g) and RNA/DNA ratio in both muscle and liver. Protein synthesis capacity (PSC:RNA, microgram/protein, mg), was found significantly increased in liver but not in muscle. The possible nature of these findings is discussed.
Language of Publication
English
Unique Identifier
90371161

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MeSH Heading (Major)
Diet|*; Legumes|*; Liver|GD/*ME; Muscle Proteins|*ME; Proteins|*ME
MeSH Heading
Animal; Body Weight; DNA|BI; Male; Muscles|GD; Organ Weight; Rats; Rats, Inbred Strains; RNA|BI

Publication Type
JOURNAL ARTICLE
ISSN
0034-9402
Country of Publication
SPAIN

Record 4 from database: MEDLINE
Return To Top

Title
Muscle and liver protein synthesis and degradation in growing rats fed a raw field bean (Vicia faba L.) diet.
Author
Goena M; Santidrián S; Cuevillas F; Larralde J
Address
Departamento de FisiologÆia Humana, Facultad de Medicina, Universidad de Navarra, Pamplona, Spain.
Source
Rev Esp Fisiol, 1988 Dec, 44:4, 345-51
Abstract
Body weight gain, food intake, gastrocnemius muscle and liver weight, protein and RNA content, as well as the fractional rates of muscle and liver protein synthesis (ks, according to the method of constant infusion of L-[14C]tyrosine), growth (kg) and degradation (kd), along with RNA activity (g of protein synthesized per day/g RNA) of both organs, were determined in growing male rats fed ad libitum over a period of 10 days on 18.7% protein diets containing either casein (5% of methionine added) (control) or the raw legume field bean (Vicia faba L.) as the sole sources of protein. It has been found that as compared to control rats, those fed the raw legume diet exhibited a significant reduction in the rate of growth, muscle RNA, ks, kg, kd and RNA activity, and a significant increase in liver ks, kd and RNA activity. All differences were statistically significant at least at the 5% level. The possible nature of these findings is discussed.
Language of Publication
English
Unique Identifier
89221845

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MeSH Heading (Major)
Legumes|*ME; Liver|GD/*ME; Muscles|GD/*ME; Proteins|*ME
MeSH Heading
Animal; Diet; Male; Organ Weight; Rats; Rats, Inbred Strains; RNA|ME; Support, Non-U.S. Gov't

Publication Type
JOURNAL ARTICLE
ISSN
0034-9402
Country of Publication
SPAIN

Record 5 from database: MEDLINE
Return To Top

Title
Nutritional outcome and immunocompetence in mice fed on a diet containing raw field beans (Vicia faba, var. minor) as the source of protein.
Author
Martínez JA; Macarulla MT; Marcos R; Larralde J
Address
Department of Nutrition and Food Science, University of PaÆis Vasco, Vitoria, Spain.
Source
Br J Nutr, 1992 Sep, 68:2, 493-503
Abstract
Feeding growth mice on diets containing raw field beans (Vicia faba var. minor) as the only source of protein brought about an impairment in growth, muscle mass and liver weight. No changes in food consumption were observed, but the food intake:weight gain ratio was increased in those animals. Plasma protein, triacylglycerols and cholesterol values were not affected by the dietary treatment although serum glucose and zinc levels fell after legume intake as well as the number of circulating erythrocytes. The relative enlargement of thymus and spleen in the legume-fed mice was apparently accompanied by a reduction in the cell number and an increase in cell size, while the protein synthesis capacity followed differentiated patterns in both tissues when assessed through protein, DNA and RNA determinations. The haemagglutination titres and the number of rosette-forming cells were lower in those animals fed on the field bean diet as well as the splenic lymphocyte responses to phytohaemagglutinin, Concanavalin A or lipopolysaccharide mitogens used to evaluate the functional status of T and B lymphocytes. The present study describes, apparently for the first time in mice, the involvement of field bean intake in some immunological disturbances affecting both humoral- and cell-mediated aspects of the immune response.
Language of Publication
English
Unique Identifier
93075677

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MeSH Heading (Major)
Diet|*; Growth|*PH; Immunocompetence|*PH; Legumes|*/CH; Nutritional Status|*PH; Plant Proteins|*AD
MeSH Heading
Animal; Erythrocyte Count; Hemagglutination Tests; Liver|AH; Male; Mice; Mice, Inbred Strains; Muscles|AH; Organ Weight|PH; Spleen|AH; Support, Non-U.S. Gov't; Thymus Gland|AH

Publication Type
JOURNAL ARTICLE
ISSN
0007-1145
Country of Publication
ENGLAND

Record 6 from database: MEDLINE
Return To Top

Title
Response of muscle, liver and whole-body protein turnover to two different sources of protein in growing rats.
Author
Martínez JA; Goena M; Santidrián S; Larralde J
Address
 
Source
Ann Nutr Metab, 1987, 31:3, 146-53
Abstract
A significant impairment in growth rate, food efficiency and weight of the gastrocnemius muscle was observed in rats fed a raw legume as the source of protein compared to casein-fed animals. No appreciable differences in chemical composition of the carcass were found. The source of dietary protein did not influence the ratio protein/DNA, DNA concentration or protein-synthesizing capacity (RNA/protein). The slower weight gain of animals fed the legume diet was attributed to a lower muscle protein synthesis, mediated by a depression of muscle RNA activity (grams protein synthesized/gram RNA) rather than changes in myofibrillar protein breakdown. In contrast liver protein synthesis appeared to be slightly increased in the legume-fed animals.
Language of Publication
English
Unique Identifier
87240061

Return To Top


MeSH Heading (Major)
Dietary Proteins|*PD; Liver|*ME; Muscles|*ME; Proteins|*ME
MeSH Heading
Animal; Body Weight|DE; Caseins|PD; Eating|DE; Legumes; Male; Rats; Rats, Inbred Strains; RNA|ME; Support, Non-U.S. Gov't; Vegetable Proteins|PD

Publication Type
JOURNAL ARTICLE
ISSN
0250-6807
Country of Publication
SWITZERLAND

Record 7 from database: MEDLINE
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Title
Synthesis, formation, and occurrence of contaminants in biotechnologically manufactured L-tryptophan.
Author
Simat TJ; Kleeberg KK; Müller B; Sierts A
Address
Department of Food Chemistry, University of Hamburg. thomas_simat@public.uni-hamburg.de
Source
Adv Exp Med Biol, 1999, 467:, 469-80
Abstract
The pattern of contaminants in pharmaceutical and feed grade L-tryptophan (Trp) was investigated in a market survey of 22 lots of 6 different manufacturers. To date, 5 case associated contaminants in Showa Denko tryptophan (SD-Trp) known to cause the autoimmune disease eosinophilia-myalgia syndrome (EMS) have been structurally elucidated: 3a-hydroxy-1,2,3,3a,8,8a-hexahydropyrroloindole-2-carboxylic acid (PIC), an indoline compound, is one of the most abundant degradation compounds of unbound Trp during oxidative treatment. 2-(3-indolylmethyl)-L-tryptophan (IMT) and 2-(2-hydroxyindoline)-tryptophan (HIT) are both 2-substituted Trp-derivatives. IMT was synthesized by the reaction of Trp and indole-3-methanol or indole-3-acetaldehyde, respectively. From this finding it is proposed that Trp-metabolites can decompose under formation of transitional, mesomerism-stabilized cations that react with excess Trp to yield 2-substituted Trp derivatives. The decomposition of Trp-metabolites could be induced by elevated or low pH-values that occur during the downstream processing of the Trp fermentation broth. IMT was detected in pharmaceutical-grade and feed-grade Trp in amounts of < 20-1,400 mg/kg. 1,1'-Ethylidenebis-(L-tryptophan) (EBT) is formed from acetaldehyde and Trp under acidic conditions and serves as a marker for EMS-suspicious Trp. 3-(Phenylamino)alanine (PAA) is the only not Trp derived case associated contaminant. Low amounts of PAA (20 mg/kg) could be detected in feed-grade Trp of one manufacturer. Non-EMS correlated 1,2,3,4-tetrahydro-beta-carboline-3-carboxylic acids of Trp and formaldehyde, acetaldehyde and indole-3-acetaldehyde could be detected in the examined Trp raw materials (< 10-13,500 mg/kg). In order to guarantee the safety of Trp containing drugs the amount of EBT (< 10 mg/kg Trp) and the sum of UV220 nm detectable contaminants (< 400 mg/kg Trp) are limited by the European authorities.
Language of Publication
English
Unique Identifier
20185868

Return To Top


MeSH Heading (Major)
Biotechnology|*ST; Drug Contamination|*; Tryptophan|*AA/*CH/CS/ST
MeSH Heading
Animal Feed; Eosinophilia-Myalgia Syndrome|CI; Human; Protein Binding; Quality Control; Serum Albumin|ME

Publication Type
JOURNAL ARTICLE
ISSN
0065-2598
Country of Publication
UNITED STATES

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