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   <subfield code="a">Presence of cardiac α-myosin correlates with histochemical myosin Ca2+ ATPase activity in rabbit masseter muscle</subfield>
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   <subfield code="c">[J. Bredman, W. Weijs, A. Moorman]</subfield>
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   <subfield code="a">Summary: A combined enzyme-histochemical (ATPase reactivity) and immunohistochemical study has been performed on sections of rabbit masseter muscle. The majority of the fibres previously designated as type IIC and/or type I according to their ATPase activity were found to contain ‘cardiac' α-myosin heavy chain in addition to other myosin heavy chains. All α-myosin heavy chain-containing fibres reveal ATPase activity after pre-incubation at pH 4.2-4.6 similar to that of the classical type I fibres, while in that pH range, limb type IIC fibres show intermediate ATPase activity. One group of these fibres reveal ATPase activity after pre-incubation at pH 10.1-10.3 as well, but not at pH 10.4-10.5. These fibres contain exclusively either α- or α- and I-myosin heavy chains but do not contain the IIA-myosin heavy chain. The second part of the fibres reveals ATPase activity after treatment within the whole alkaline pre-incubation range (pH 10.1-10.5) and these fibres contain α-myosin and IIA-myosin but no, I-myosin heavy chain. It is concluded that the classical IIC fibre type is not present in the rabbit masseter muscle. Furthermore, ATPase reactivity does not allow us to distinguish fibres on their myosin heavy chain content in rabbit masseter muscle.</subfield>
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   <subfield code="D">J.</subfield>
   <subfield code="u">Department of Functional Anatomy, Academic Centre for Dentistry, Amsterdam (ACTA), The Netherlands</subfield>
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