Purification and Characterization of Human Adrenomedullin Binding Protein-1

Purification and characterization of antiviral protein from silkworm fecal matter

Antiviral proteins (AVP), present in silkworm fecal matter, show activity against nuclear polyhedrosis virus (NPV) in vitro and in vivo. The extract of silkworm fecal matter prepared in phosphate buffer solution of pH 7.5 was subjected to 50% solid ammonium sulfate precipitation to enrich AVP, then which was dialyzed. The dialysate was applied to the column containing silica gel-G, the column e...

Adrenomedullin Binding Protein-1 Modulates Vascular Responsiveness to Adrenomedullin During the Late Stage of Sepsis

Purification and characterization of an Acanthamoeba nuclear actin- binding protein

Immunolocalization of monoclonal antibodies to Acanthamoeba myosin I showed a cross-reactive protein in nuclei (Hagen, S. J., D. P. Kiehart, D. A. Kaiser, and T. D. Pollard. 1986. J. Cell Biol. 103:2121-2128). This protein is antigenically related to myosin I in that nine monoclonal antibodies and three polyclonal antibodies are cross-reactive. However, studies with affinity-purified antibodies...

Adrenomedullin binding protein-1 modulates vascular responsiveness to adrenomedullin in late sepsis.

Adrenomedullin (AM), a potent vasodilatory peptide, plays an important role in initiating the hyperdynamic response during the early stage of sepsis. Moreover, the reduced vascular responsiveness to AM appears to be responsible for the transition from the early, hyperdynamic to the late, hypodynamic phase of sepsis. Although the novel specific AM binding protein-1 (AMBP-1) enhances AM-mediated ...

Purification and partial characterization of cellular retinol-binding protein from human liver.

Cellular retinol-binding protein (CRBP) has been purified to homogeneity from normal human liver. The procedures in the purification involved primarily gel filtration and ion exchange chromatography, resulting in a 3000-fold purification with greater than 40% yield. The protein is a single:polypeptide chain with molecular weight of 14,800. The protein binds retinol in a manner which considerabl...