Characterization of Secondary Structure of Neocarzinostain Apoprotein

• Published in: Chemical & pharmaceutical bulletin Vol. 37; no. 11; pp. 3078 - 3082
• Main Authors: SAITO, Kunihito, EDO, Kiyoto, ISHIDA, Nakao, MIZUGAKI, Michinao, SATO, Yukio, AKIYAMA-MURAI, Yuriko, KOIDE, Yoshio
• Format: Journal Article
• Language: English
• Published: Tokyo The Pharmaceutical Society of Japan 25.11.1989; 公益社団法人日本薬学会; Japan Science and Technology Agency
• Subjects: chromophore environment; neocarzinostatin; neocarzinostatin-apoprotein; neocarzinostatin-chromophore; parallel pleated structure; secondary structure
• ISSN: 0009-2363; 1347-5223
• DOI: 10.1248/cpb.37.3078

Characteristics of the secondary structure of neocarzinostatin apoprotein (apo-NCS) were examined by various means. Gaussian analysis of the Fourier-transform infrared (FT-IR) curve and curve-fitting of the circular dichroism (CD) spectrum for apo-NCS revealed that this peptide was abundant in β-structures. In the presence of sodium dodecyl sulfate (SDS), the CD bands of NCS originating from phenylalanyl, tyrosyl, and cystinyl residues decreased, indicating a conformational change around the chromophore (NCS-chr). On the other hand, apo-NCS, in the SDS system, showed no change of these bands. We showed that the major parts of the protein moiety consist of β-structures by measurements of the FT-IR and CD spectra of apo-NCS and a prediction of the secondary structure based on the amino acid sequence of the peptide. It seems that properties of the protein may be important to the hydrophobic interaction between NCS-chr and apo-NCS.