Neraal R, Hamm R
Z Lebensm Unters Forsch. 1977 Mar 21;163(3):208-12. doi: 10.1007/BF01459860.
The diphosphatase (DPase) activity of minced bovine muscle decreased during storage of the intact muscle post mortem (p.m.) but there was only little change after development of rigor mortis. The drop in pH p.m. seems to be not the only reason for the decrease in DPase activity. In the postrigor muscle the DPase activity, measured at pH greater than 6, increased during the breakdown of DP. The rise of activity was the slower the longer the muscle was stored. The result of a mathematical regression analysis, developed for the kinetic study of this anomaly in the breakdown of DP, indicates that a certain mechanism of activation of the initially inactive DPase in muscle exists.
牛肌肉碎末的二磷酸酶(DPase)活性在宰后完整肌肉储存期间会下降,但尸僵形成后变化很小。宰后pH值下降似乎不是DPase活性降低的唯一原因。在尸僵后肌肉中,在pH值大于6时测得的DPase活性在DP分解过程中增加。肌肉储存时间越长,活性上升越慢。为研究DP分解过程中的这种异常动力学而进行的数学回归分析结果表明,肌肉中存在某种激活最初无活性的DPase的机制。