ABSTRACT
We investigated the relationship between stress responsiveness and meat quality in cattle. The cattle were 16-19-month-old Mixed (n=37, 303 kg) or Non-mixed (n=23, 279 kg) Friesian bulls and Friesian cull cows (1.5-7 years) that were classified Unfinished (n=133, 195 kg) or Finished for 3 months (n=34, 252 kg). A portion of m. longissimus lumborum (LL) muscle was obtained from consecutive animals for a single days slaughter of 227 cattle processed through a hot boning plant. Catecholamines were obtained from bladder urine. Ultimate pH, lactate, glycogen, glycolytic potential and representative sarcomere lengths were determined from 20-h muscle samples. Shear force measurements were from meat aged at 15 °C for 20 and 90 h. Urinary noradrenaline was similar between Mixed (14.86 ng/µmol creatinine) and Non-mixed bulls (14.07 ng/µmol creatinine) and Finished cows (15.24 ng/µmol creatinine) and elevated in the Unfinished cows (22.28 ng/µmol creatinine). Urinary adrenaline was higher in Mixed bulls (9.5 ng/µmol creatinine) than Non-mixed bulls (5.7 ng/µmol creatinine) and higher in both Unfinished cows (16.67 ng/µmol creatinine) and Finished cows (14.19 ng/µmol creatinine). For bulls that are growing well on-farm, with a only short period of fasting prior to slaughter, pH(u) is a good predictor of meat tenderness. In this situation, stressors that lower muscle glycogen pre-slaughter can have a significant effect on meat shear force, and individual animals with elevated urinary adrenaline were the most susceptible. However, in the case of cows, adrenaline responses are not necessarily associated with glycogen depletion and pH(u) is less affected than for bulls. Furthermore, the ability of meat to tenderise fully, related to reduced proteolytic turnover, is reduced in nutritionally compromised animals such as the Unfinished cows.
ABSTRACT
The types and subunit composition of cAMP-dependent protein kinases in soluble rat ovarian extracts were investigated. Results demonstrated that three peaks of cAMP-dependent kinase activity could be resolved using DEAE-cellulose chromatography. Based on the sedimentation of cAMP-dependent protein kinase and regulatory subunits using sucrose density gradient centrifugation, identification of 8-N3[32P]cAMP labeled RI and RII in DEAE-cellulose column and sucrose gradient fractions by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and Scatchard analysis of the cAMP-stimulated activation of the eluted peaks of kinase activity, the following conclusions were drawn regarding the composition of the three peaks of cAMP-dependent protein kinase activity: peak 1, eluting with less than or equal to 0.05 M potassium phosphate, consisted of the type I form of cAMP-dependent protein kinase; peak 2, eluting with 0.065-0.11 M potassium phosphate, consisted of free RI and a type II tetrameric holoenzyme; peak 3, eluting with 0.125 M potassium phosphate, consisted of an apparent RIIC trimer, followed by the elution with 0.15 M potassium phosphate of free RII. The regulatory subunits were confirmed as authentic RI and RII based upon their molecular weights and autophosphorylation characteristics. The more basic elution of the type II holoenzyme with free RI was not attributable to the ionic properties of the regulatory subunits, based upon the isoelectric points of photolabeled RI and RII and upon the elution location from DEAE-cellulose of RI and RII on dissociation from their respective holoenzymes by cAMP. This is the first report of a type II holoenzyme eluting in low salt fractions with free RI, and of the presence of an apparent RIIC trimer in a soluble tissue extract.
