Modification of the C-terminal octapeptide of cholecystokinin with a high-specific-activity iodinated imidoester: preparation, characterization, and binding to isolated pancreatic acinar cells |
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Authors: | M Praissman R S Izzo J M Berkowitz |
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Institution: | 1. Department of Pathology, University of Washington, School of Medicine, Seattle, Washington 98195 USA;2. the Center for Research in Oral Biology, University of Washington, School of Medicine, Seattle, Washington 98195 USA |
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Abstract: | Proteoglycans were separated by high-performance liquid chromatography (HPLC), using two coupled Aquapore columns containing glycerylpropylsilane groups covalently linked to large-pore (50–100 nm) silica spheres. This two-column HPLC system was effective in separating cartilage proteoglycan aggregates and monomers, without altering their biochemical integrity. This system was also effective in resolving small amounts of isotopically labeled proteoglycans synthesized by cultured mammalian cells. The small sample size, short analysis time, and high reproducibility represent improvements in the study of proteoglycans over conventional soft-gel chromatography. |
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Keywords: | To whom correspondence and reprint requests should be addressed at the Department of Pathology University of Pennsylvania School of Medicine 3400 Spruce Street Philadelphia Pennsylvania 19104 |
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