. Cytochemistry: a critical approach. Cells. SECRETION BY CONTRACTILE PROTEINS 73 concentration, indicating that there is a limited supply of the transporting molecules in the cell membrane. If we consider Goldacre's proposal in the light of Osterhout's work and of the studies on phosphatase, it appears that we can meet the requirements of the situation by a model such as that in- Adsorption_ centre -*~e U d +-U Plasma membrane -Contractile protein ^•Phosphatase or phosphokinase enzymic centre or other phosphate ester. ^~ Enzymic centre Adsorption centre 0or 0OPO3H2 Fig. 4. Diagram to i
. Cytochemistry: a critical approach. Cells. SECRETION BY CONTRACTILE PROTEINS 73 concentration, indicating that there is a limited supply of the transporting molecules in the cell membrane. If we consider Goldacre's proposal in the light of Osterhout's work and of the studies on phosphatase, it appears that we can meet the requirements of the situation by a model such as that in- Adsorption_ centre -*~e U d +-U Plasma membrane -Contractile protein ^•Phosphatase or phosphokinase enzymic centre or other phosphate ester. ^~ Enzymic centre Adsorption centre 0or 0OPO3H2 Fig. 4. Diagram to illustrate one of the possible mechanisms for transport- ing the substance 0 across a membrane as the result of the action of a contractile enzyme. dicated in Fig. 4. This model is based upon the view that the secretory activity is performed by the folding of a contractile protein, and that the contraction is brought about by reaction of the protein with a substance such as (adenosine triphos- phate), as is the case with actomyosin. The phosphatase thus represents an enzymic centre through which the energy of is transferred to the contractile protein. In this model, as indi- cated on the upper part of the figure, the initial configuration of the protein has one part of an extended chain on the cyto-. Please note that these images are extracted from scanned page images that may have been digitally enhanced for readability - coloration and appearance of these illustrations may not perfectly resemble the original Danielli, J. F. (James Frederic), 1911-. New York Wiley
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