Väänänen H K, Kumpulainen T, Korhonen L K
J Histochem Cytochem. 1982 Nov;30(11):1109-13. doi: 10.1177/30.11.6216280.
The localization of carbonic anhydrase (CA) was studied in rat skeletal muscles with the use of immunohistochemical (peroxidase-antiperoxidase) method. CA was observed in all those fibers that also showed pH 4.3 stable actomyosin adenosine triphosphatase activity (type I fibers), but the reverse did not necessarily hold. More specifically, CA was apparently localized in I-bands, and a weak reaction was also observed in sarcolemma. The function of CA in muscle fibers is possibly connected with the greater demands on CO2 transport and buffer system in muscles adapted to long-lasting contractions.
利用免疫组织化学(过氧化物酶-抗过氧化物酶)方法研究了大鼠骨骼肌中碳酸酐酶(CA)的定位。在所有那些也显示出pH 4.3稳定的肌动球蛋白三磷酸腺苷酶活性的纤维(I型纤维)中观察到了CA,但反之则不一定成立。更具体地说,CA显然定位于I带,并且在肌膜中也观察到微弱反应。CA在肌纤维中的功能可能与适应持久收缩的肌肉对二氧化碳运输和缓冲系统的更高需求有关。