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(Yoong Ho Lim),(Mi Na Oh),(K . Hun Mok) 한국응용생명화학회 1998 Applied Biological Chemistry (Appl Biol Chem) Vol.41 No.8
The conformations of human insulin precursors, proinsulin and preproinsulin, are described in terms of molecular dynamics simulations. Despite the presence of the C-peptide and/or the signal peptide, molecular dynamics calculations utilizing the hydration shell model over a period of 500 ps indicate that the native conformations of the A and B chains are well conserved in both cases. These results further support the NMR spectroscopy results that the C-peptide is relatively disordered and does not influence the overall conformation of the native structure. The robustness of the native structure as demonstrated by experiment and simulation will permit future protein engineering applications, whereby the expression or purification yields can be improved upon sequence modification of the C-peptide and/or the signal peptide.
A Comparison of Three Dimensional Structures of Biosynthesized Preproinsulin and Insulin Using NMR
(Yoong Ho Lim),(Mi Na Oh),(K . Hun Mok) 한국응용생명화학회 1998 Applied Biological Chemistry (Appl Biol Chem) Vol.41 No.8
The solution conformation of the human insulin precursor, preproinsulin, is described in terms of NMR spectral data. NMR experiments were performed on preproinsulin, whose structure was compared with the NMR structure of native human insulin. Despite the presence of the C-peptide and/or the signal peptide, secondary structure analyses indicate that the native structures of the A and B chains are well conserved even in preproinsulin. The observed relative robustness of the native structure in precursor forms permits further protein engineering experiments where the C-peptide or N-terminal signal sequence can be altered for the purpose of increasing expression or purification yields when producing recombinant human insulin.
백남진,강재구,김달현,목헌,김제학,김현수,Baek, Nam-Jin,Kang, Jae-Ku,Kim, Dal-Hyun,Mok, K.-Hun,Kim, Je-Hak,Kim, Hyun-Su 한국독성학회 1997 Toxicological Research Vol.13 No.3
Antigenic potential of genetically engineered human granulocyte colony-stimulating factor (CJ-50001) was assessed in guinea pigs and mice. In active systemic anaphylaxis (ASA) test, although CJ-50001 at 50 $\mu\textrm{g}$ /head induced anaphylactic responses, CJ-50001 5 $\mu\textrm{g}$ /head alone or 50 $\mu\textrm{g}$ / head with adjuvant did not induce anaphylactic responses. In passive systemic anaphylaxis test (PCA) or passive hemagglutination test (PHA), CJ-50001 did not induce positive responses. It is concluded that, in light of the fact that CJ-50001 was antigenic only in ASA but not in PCA or PHA and also that CJ-50001 is a foreign human recombinant protein to guinea pigs, CJ-50001 may not induce systemic allergic react-ion in its clinical use in human.