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1.
Poult Sci ; 93(1): 187-93, 2014 Jan.
Article in English | MEDLINE | ID: mdl-24570438

ABSTRACT

The physico-chemical quality attributes of meat from broilers with significant differences in growth rate were investigated in this study. Two chicken populations from a random mating broiler control population were established as a slow-growing subpopulation (SG) with an average growth rate of 229 g/wk and a fast-growing subpopulation (FG) with an average growth rate of 319 g/wk. The initial pH at 15 min and final pH after 24 h were higher (P < 0.05) in breast muscle from FG than muscle from the SG population. Muscle from the SG had higher (P < 0.05) L* and b* of 57.0 and 11.2, compared with L* and b* of 55.8 and 10.5 from the FG. Although no difference in a* was observed, hue angle was different (P < 0.05) at 52.7 and 50.4 in FG and SG populations, respectively. Water-holding capacity was 25 to 27% and not different between the populations, but 5-d drip loss at 8.48% was higher (P < 0.05) in the muscle from the SG compared with the FG at 6.44%. Cook yield was higher (P < 0.05) in the FG muscle at 86.92% compared with the SG muscle at 85.96%. There was a positive correlation of +0.20 between pH difference and drip loss only in the FG. Significantly higher (P < 0.05) cook yields were observed in muscle from FG than SG chickens. The lower weight, higher L* value, and lower initial and final pH values in the SG population, coupled with higher drip loss and lower cook yield, likely result from differences in growth rate.


Subject(s)
Chickens/growth & development , Chickens/genetics , Muscle, Skeletal/physiology , Animals , Female , Male
2.
J Biol Chem ; 252(3): 835-9, 1977 Feb 10.
Article in English | MEDLINE | ID: mdl-14135

ABSTRACT

Streptococcus faecalis 8043 concentrates extracellular [3H]pyridoxal or [3H]pyridoxamine primarily as the corresponding 5'-phosphates. Accumulation of pyridoxamine requires an exogenous energy source and is inhibited by glycolysis inhibitors. A membrane potential is not required for transport of pyridoxamine, and an artificially generated potential does not drive uptake in this organism. Based on this and other evidence, it is concluded that S. faecalis accumulates pyridoxamine by facilitated diffusion in conjunction with trapping by pyridoxal kinase. Pyridoxamine-P is not concentrated, but equilibrates with that provided externally. Lactobacillus casei 7469 concentrates radioactivity only from pyridoxal, which appears internally as pyridoxal-P, suggesting that it too absorbs the vitamin by facilitated diffusion plus trapping. The specificity of the growth requirement of S. faecalis and L. casei for vitamin B6 parallels the specificity of the transport systems for this vitamin in these organisms. Lactobacillus delbrueckii 7469, however, which specifically requires pyridoxamine-P or pyridoxal-P for growth, accumulates both these compounds and pyridoxine-P from the medium, apparently by active transport, but not pyridoxine, pyridoxamine, or pyridoxal. While pyridoxal-P and pyridoxamine-P are interconvertible in this organism, pyridoxine-P is not further metabolized, thus accounting for the specificity of the growth requirement. These and previous results show (a) that different organisms may employ quite different transport machinery in utilization of a given external nutrient, and (b) that the specificity of the growth requirement for a given form of a vitamin frequently arises from the specificity of transport, but that internal metabolism of the compounds also plays a significant role in some organisms.


Subject(s)
Enterococcus faecalis/metabolism , Lacticaseibacillus casei/metabolism , Lactobacillus/metabolism , Pyridoxamine/metabolism , Pyridoxine/metabolism , Biological Transport, Active , Enterococcus faecalis/drug effects , Hydrogen-Ion Concentration , Kinetics , Membrane Potentials , Potassium/pharmacology , Sodium/pharmacology , Uncoupling Agents/pharmacology
3.
J Biol Chem ; 251(4): 1052-6, 1976 Feb 25.
Article in English | MEDLINE | ID: mdl-2599

ABSTRACT

Salmonella typhimurium LT2 concentrates radioactivity intracellularly from [3H]pyridoxal or [3H]pyridoxine up to 25 times the external concentration. After 1 min of uptake intracellular radioactivity is found as phosphorylated vitamin B6. The process is sensitive to temperature and is maximally active at pH 8.1, but under the conditions tested it is insensitive to monovalent cations or metabolic inhibitors, and does not require an exogenous energy source. The Km values for uptake of pyridoxine and pyridoxal are 2.0 x 10(-7) M and 1.2 x 10(-7) M, respectively; [3H]pyridoxamine is not transported. Evidence is presented for an uptake mechanism involving facilitated diffusion followed by trapping by pyridoxal kinase. S. typhimurium also appears to lack a periplasmic binding protein for vitamin B6.


Subject(s)
Pyridoxine/metabolism , Salmonella typhimurium/metabolism , Biological Transport, Active , Hydrogen-Ion Concentration , Kinetics , Osmotic Pressure , Pyridoxal/metabolism , Salmonella typhimurium/drug effects , Toluene/pharmacology
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