Bais R, Edwards J B
Crit Rev Clin Lab Sci. 1982;16(4):291-335. doi: 10.3109/10408368209107030.
Creatine kinase is present in significant concentrations in skeletal muscle and cardiac muscle and to a lesser extent in gastrointestinal tract and brain tissue. The enzyme has been purified from a variety of tissues and an examination of its kinetic and physical properties reveal that the enzyme consists of two subunits and can exist as three isoenzymes containing essential cysteine residues. These properties are important in understanding its stability, the assay conditions, and the techniques used to identify the different isoenzymes. The relationship between the properties and the determination of the enzyme in biological fluids will be a main thrust of the review. Creatine kinase activity in serum rises rapidly in conditions such as acute myocardial infarction and trauma to skeletal muscle. However, the interpretation of such increases is dependent upon a sound knowledge of the factors which influence both the total and isoenzyme activities. The nature of these factors will be discussed in detail.
肌酸激酶在骨骼肌和心肌中大量存在，在胃肠道和脑组织中含量较少。该酶已从多种组织中纯化出来，对其动力学和物理性质的研究表明，该酶由两个亚基组成，可作为三种含有必需半胱氨酸残基的同工酶存在。这些特性对于理解其稳定性、测定条件以及用于鉴定不同同工酶的技术非常重要。特性与生物体液中酶的测定之间的关系将是本综述的主要内容。在急性心肌梗死和骨骼肌创伤等情况下，血清中的肌酸激酶活性会迅速升高。然而，对这种升高的解释取决于对影响总活性和同工酶活性的因素的充分了解。将详细讨论这些因素的性质。
