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Nerve growth factor: Subunit interactions in the mouse submaxillary gland 7S complex

1982; Wiley; Volume: 8; Issue: 2-3 Linguagem: Inglês

10.1002/jnr.490080204

1097-4547

Robert E. Silverman, Ralph Bradshaw,

Pain Mechanisms and Treatments

Abstract Sedimentation velocity analyses of the isolated subunits of mouse 7S nerve growth factor (NGF) and their binary complexes have been performed. The 2.5S (β) form of NGF binds 2 α subunits independent of the presence of γ subunits. Two γ subunits are also complexed by 2.5S NGF; however, this interaction is dependent on the presence of a carboxyl terminal arginine residue on the β polypeptide chain. The partial loss of this residue in 2.5S NGF preparations results in a ternary complex(es) with a reduced sedimentation coefficient(s). The two binary complexes formed (α 2 ‐β and β‐γ 2 ) show markedly different pH stability profiles. The α and γ subunits do not form a demonstrable complex, but apparently can interact in the ternary complex to render it more stable than the sum of the α‐β and β‐γ interactions.