Erroneous interpretations which may result from application of the "myofibrillar ATPase" histochemical procedure to developing muscle.
Erroneous interpretations which may result from application of the "myofibrillar ATPase" histochemical procedure to developing muscle.
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将“肌原纤维 ATP 酶”组织化学程序应用于发育中的肌肉可能会导致错误的解释。
DOI：
10.1016/0014-4886(72)90042-8
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发表时间：
1972
影响因子：
5.3
通讯作者：
F. Samaha
中科院分区：
文献类型：
--
作者：
L. Guth;F. Samaha
在成年哺乳动物的肌肉中，肌动球蛋白ATP酶（AM-ATP酶）活性，通过生物化学或组织化学估计，与收缩速度成比例，慢肌具有低酶活性，快肌具有高活性。然而，新生哺乳动物的肌肉是缓慢收缩的，但它们通过目前用于证明AM-ATP酶活性的组织化学程序强烈应变。生物化学和组织化学方法已被应用于新生和缓慢和快速的成年兔肌肉，以确定是否新生肌纤维的强烈组织化学反应实际上是由于定量高AM-ATP酶活性。虽然大多数纤维的1，5和10日龄的兔子一样强烈的成人快肌纤维染色，肌动球蛋白的ATP酶活性分离的5和10日龄的肌肉实际上是非常低的，是相同的成人慢肌和快肌的约25%。新生肌纤维的强染色可以通过它们的ATP酶的pH稳定性、肌原纤维包装的差异和其他ATP酶的染色来解释。成人慢肌的AM-ATP酶是碱不稳定的，而成人快肌和新生肌的AM-ATP酶是碱稳定的。由于AM-ATP酶的组织化学反应需要碱性条件（pH 9.4），新生儿肌肉染色强度大于成人慢肌，即使这两种组织的特异性活性相似。我们的结论是，AM-ATP酶的组织化学方法并不一定揭示酶活性的水平，并可能导致错误的结论，从定量解释组织化学观察。
In muscles of adult mammals, actomyosin ATPase (AM-ATPase) activity, estimated either biochemically or by histochemistry, is proportional to the speed of contraction, slow muscles having low enzymatic activity and fast muscles having high activity. However, the muscles of newborn mammals are slowly contracting, yet they strain intensely by the histochemical procedure currently used to demonstrate AM-ATPase activity. Biochemical and histochemical methods have been applied to newborn and to slow and fast adult rabbit muscle to ascertain whether the intense histochemical reactivity of newborn muscle fibers is actually due to a quantitatively high AM-ATPase activity. While the majority of fibers of 1, 5 and 10-day-old rabbits stained as intensely as adult fast muscle fibers, the ATPase activity of actomyosin isolated from the 5 and 10-day-old muscles was in fact very low, being the same as that of adult slow muscle and approximately 25% of that of fast muscle. The intense staining of the neonatal fibers can be explained by the pH stability of their ATPase, the difference in packing of myofibrils and the staining of other ATPases. The AM-ATPase of adult slow muscle is alkali-labile, whereas that of adult fast muscle and of neonatal muscle is alkali-stable. Inasmuch as the histochemical reaction for AM-ATPase requires alkaline conditions (pH 9.4), the neonatal muscle stains with greater intensity than does adult slow muscle even though the specific activity of the two tissues is similar. We conclude that the histochemical method for AM-ATPase does not necessarily reveal the level of enzymatic activity and that erroneous conclusions may result from the quantitative interpretation of histochemical observations.