Thermostability of purified human pancreatic α-amylase is increased by the combination of Ca2+ and human serum albumin

Tessier, Arthur J.; Dombi, George W.; Bouwman, David L.

doi:10.1016/0009-8981(96)06316-4

Cited by 5 publications

(2 citation statements)

References 18 publications

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“…Another possible hypothesis is that albumin directly stabilizes viral capsids. This is based on known protein-stabilizing properties of albumin ; it protects thermolabile proteins, probably via hydrophobic interactions (Chang & Mahoney, 1995 ;Tessier et al, 1996). Moreover, the degree of surface hydrophobicity of proteins is thought to be a major determinant of this stabilizing effect.…”

Section: Albumin Inhibits Uncoatingmentioning

confidence: 99%

Serum albumin inhibits echovirus 7 uncoating.

Ward

Powell

Evans

et al. 1999

Journal of General Virology

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Echoviruses induce a wide spectrum of diseases in man, the most severe being meningitis. In neonates, however, a severe systemic infection can be observed, leading to death. Serum albumin is the most abundant protein in plasma and most interstitial fluids, and its functions include osmoregulation and transport and delivery of hydrophobic molecules such as fatty acids and steroids. The results of cold-synchronized one-step growth analysis of echovirus 7 infection and sucrose-gradient analysis of A-particles suggest that physiological concentrations of albumin block echovirus 7 infection by inhibiting uncoating. The blockage was reversible and was still effective when albumin was added 30 min after virus adsorption. Inhibition of uncoating was confirmed by using rhodanine, a known specific inhibitor of echovirus uncoating. After removal of the albumin blockage, addition of rhodanine perpetuated the inhibition. Serum and interstitial albumin concentrations may limit echovirus infection in vivo and thereby act as an extracellular determinant for echovirus tropism.

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