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Cited by 191

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Two related but distinct forms of the Mr 36,000 tyrosine kinase substrate (calpactin) that interact with phospholipid and actin in a Ca2+-dependent manner.

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Glenney, J·1986·Proceedings of the National Academy of Sciences

Abstract

A method was devised that allows the identification of proteins related to the Mr 36,000 tyrosine kinase substrate calpactin based on their ability to interact with actin and phospholipid in a calcium-dependent manner. Two distinct proteins, detected in human A431 cells and fibroblasts, were resolved by two-dimensional gel electrophoresis. One of these proteins (calpactin I) appears identical to the Mr 34,000-39,000 substrate of the pp60src tyrosine kinase and the second (calpactin II) reacts with antibodies to the Mr 35,000 substrate of the epidermal growth factor receptor. Both proteins interact with phospholipid and actin, are rather basic, and share structural and antigenic determinants. A major difference between the two proteins is noted in their state of association with the Mr 10,000 light chain; i.e., calpactin I is associated with the light chain while calpactin II is not.

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Metadata

Authors
Glenney, J.
Venue
Proceedings of the National Academy of Sciences
Published
1986-06
Volume
83
Issue
12
Pages
4258-4262
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2026581597
Cited by
191
References
0
FWCI
14.71
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Two related but distinct forms of the Mr 36,000 tyrosine kinase substrate (calpactin) that interact with phospholipid and actin in a Ca2+-dependent manner. https://app.cochat.ai/papers/10.1073/pnas.83.12.4258
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Glenney, J. (1986). Two related but distinct forms of the Mr 36,000 tyrosine kinase substrate (calpactin) that interact with phospholipid and actin in a Ca2+-dependent manner. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.83.12.4258

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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.