67 k calcimedin (67 kDa) is distinct from p67 calelectrin and lymphocyte 68 kDa Ca2+-binding protein

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An immunological and biochemical comparison of 67 kDa calcimedin and 67 kDa calelectrin.

The 67 kDa calcimedin is a Ca2+-binding protein isolated from several muscle tissues. A recent report [Morse & Moore (1988) Biochem. J. 251, 171-174] indicated that the 67 kDa calcimedin is distinct from 67 kDa calelectrin, which is purified from various non-muscle cells. In the present study we have purified the 67 kDa protein from bovine aorta (i.e. 67 kDa calcimedin) and liver (i.e. 67 kDa c...

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Differential tissue expression of three 35-kDa annexin calcium-dependent phospholipid-binding proteins.

We have purified three 35-kDa calcium- and phospholipid-binding proteins from rat liver. These three calcimedins bind to phosphatidylserine in a calcium-dependent manner and have been termed 35 alpha, 35 beta, and 35 gamma based on their relative charge as determined by isoelectric focusing. Purification of the three 35-kDa calcimedins is achieved by phenyl-Sepharose, ion exchange, and gel filt...

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The 37/67 kDa laminin receptor (LR) inhibitor, NSC47924, affects 37/67 kDa LR cell surface localization and interaction with the cellular prion protein.

The 37/67 kDa laminin receptor (LR) is a non-integrin protein, which binds both laminin-1 of the extracellular matrix and prion proteins, that hold a central role in prion diseases. The 37/67 kDa LR has been identified as interactor for the prion protein (PrP(C)) and to be required for pathological PrP (PrP(Sc)) propagation in scrapie-infected neuronal cells, leading to the possibility that 37/...

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Interactions between PrP(c) and other ligands with the 37-kDa/67-kDa laminin receptor.

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Interactions of a laminin-binding peptide from a 33-kDa protein related to the 67-kDa laminin receptor with laminin and melanoma cells are heparin-dependent.

A laminin-binding peptide (peptide G), predicted from the cDNA sequence for a 33-kDa protein related to the 67-kDa laminin receptor, specifically inhibits binding of laminin to heparin and sulfatide. Since the peptide binds directly to heparin and inhibits interaction of another heparin-binding protein with the same sulfated ligands, this inhibition is due to direct competition for binding to s...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1988

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj2510171