A Research Annual by Kenneth R. Miller (Eds.)

By Kenneth R. Miller (Eds.)

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The intestinal calpactin appears to be distinct from-but related to-other tyrosine kinase substrates of the same size (Glenney, 1986~). While both 36-kd Ca++-binding and phosphorylation are brought into physiologically significant ranges by phospholipid, work to date has not commented on actin and spectrin binding. It seems likely that the Ca++ requirements for actin and TW 260/240 will fall into the physiological range in the presence of phospholipid and, if it does, then calpactin will be a leading candidate as the protein linking adherens ring and rootlet actin and TW 260/240 to the membrane.

And Watson, J. D. (1983) Molecular Biology of rhe Cell, p. 273 and Fig. 6-31. Garland, New York. Alpin, J. , and Hughes, R. C. (1981) Anal. Biochem. 113: 144-148. , and Biiechi, M. (1981) in m e Replication of Negariw Srrand Viruses (D. H. L. Bishop and R. W. ), pp. 553-558. Elsevier. Amsterdam and New York. Bearer, E. , and Friend, D. S. (1980) Roc. Natl. Acad. Sci. USA 77: 6601-6605. Branton, D. (1966) Roc. Natl. Acad. Sci. US 55: 1048-1056. , and Deamer. D. W. (1972) Frotoplasmatologia,Vol.

Nonvesicular membrane sheets such as purple membrane can be selectively oriented before chemical modification. There is a further advantage to the planar cell or membrane monolayer approach. The structure of the same sample that has been chemically or physically modified can be examined by both light and electron microscopy. Thus structural modifications can be directly compared to biochemical or biophysical observations. In most combined structure and function studies correlations are made by subdividing a sample for microscopy, biochemical assay, etc.

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