Abstract
Some lamellibranch muscles are able to maintain tension for prolonged periods with very little energy expenditure, possibly by means of a special ‘catch' mechanism. Whilst actomyosin seems to be associated with active contraction, the 'catch' might well be linked with tropomyosin
A
(
TM
A
) which is more abundant in these muscles than actomyosin (
AM
) and located in special filaments known as paramyosin. There is in fact a correlation of tropomyosin content and ‘tonic’ properties in three different portions of
Pecten maximus
adductor muscle, the striated adductor (
AM/TM
= 9:1), the translucent portion of the smooth adductor (
AM/TM
= 2:1), and the opaque portion of the latter (
AM/TM
= 1:2). A typical ‘catch’ can be demonstrated in the glycerinated fibres of the tropomyosin-rich but not in the tropomyosin-poor type by measuring fibre rigidity in presence of adenosine triphosphate (
ATP
) and Mg ions. Quick release and stretch experiments have shown that, unlike active contraction, rigidity in presence of
ATP
is not dependent on a functional
AM
system, which can be inactivated with Salyrgan, denatured with ethanol or plasticized with pyrophosphate. Instead, a change in fibre rigidity is always found to be associated with a change in the colloidal state of
TM
A
when the latter is selectively modified
in situ
, as, for example, by varying the pH between 6⋅5 and 8 or the ratio of the Mg-
ATP
chelate to 'free'
ATP
. The latter increases the solubility and the electrophoretic mobility of
TM
A
and it plasticizes artificial tropomyosin threads or the tropomyosin system
in situ
. Its action is best explained in terms of a decrease in protein-protein interaction caused by an increase in net charge due to binding, an effect which it counteracted by divalent cations which combine with
ATP
. Extra-polating these findings to the behaviour of living muscle one might tentatively suggest that the high rigidity of glycerinated tonic adductor muscle fibres in presence of Mg-
ATP
corresponds to the high muscle ‘viscosity’ of tonically contracted living molluscan muscle and that free
ATP
acts as a physiological plasticizer, inducing changes in muscle ‘viscosity’ by affecting the electrostatic tropomyosin-tropomyosin interaction either within or between the paramyosin (tropomyosin) filaments.
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