Co-precipitation of intestinal p36 with a 73-K protein and a high molecular weight factor

p36 is a major substrate of tyrosine kinases that co-localizes with spectrin in nonerythroid cells. Recent studies by Gerke & Weber [14] have shown that p36 can be isolated from intestine by selective extraction with the Ca2+-chelating agent EGTA. We now show that p36 can be re-precipitated by adding free Ca2+ to 1 mM with the co-precipitation of a high molecular weight (MW) factor and a polypeptide of 73K. The 73K protein was purified to apparent homogeneity, rabbit antibodies were raised to it and used in Western blots and immunofluorescence microscopy. The 73K protein is found in a wide range of tissues and is particularly concentrated in fibroblasts, where its distribution partially overlaps that of non-erythroid spectrin.