Membrane glycoprotein synthesis: cleavage of the signal sequence in the absence of glycosylation |
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Authors: | Robert A Irving Theo Hofmann Hara P Ghosh |
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Institution: | Institute of Biological Chemistry, University of Padua, 35100 Padua, Italy |
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Abstract: | The controlled action of trypsin on porcine pancreatic procarboxypeptidase A releases a large activation peptide which contains the activation segment of the proenzyme. Circular dichroism studies indicate that the isolated activation peptide contains a high percentage of residues in ordered secondary structures (mainly α-helix). This result agrees with predictions of secondary structure carried out on the published amino acid sequence of the homologous rat proenzyme. Moreover, proton magnetic resonance spectroscopy shows that the peptide adopts a thermostable tertiary structure with characteristics typical of globular proteins. The results as a whole indicate that the activation segment of porcine pancreatic procarboxypeptidase A constitutes a folded structural domain. |
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Keywords: | Procarboxypeptidase A Activation segment Conformation Structural domain Circular dichroism Nuclear magnetic resonance CD circular dichroism NMR nuclear magnetic resonance RCS ring-current shifted |
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