By a News Reporter-Staff News Editor at Life Science Weekly -- Investigators discuss new findings in Enzymes and Coenzymes. According to news reporting out of Beijing, People's Republic of China, by NewsRx editors, research stated, "Cathepsin D (CD) plays an important role in both biological and pathological processes, although the cleavage characteristics and substrate selection of CD have yet to be fully explored. We employed liquid chromatography-tandem mass spectrometry (LC-MS/MS) to identify the CD cleavage sites in bovine serum albumin (BSA)."
Our news journalists obtained a quote from the research from the Beijing Institute of Genomics, "We found that the hydrophobic residues at P1 were not only a preferential factor for CD cleavage but that the hydrophobicity at P1' also contributed to CD recognition. The concept of hydrophobic scores of neighbors (HSN) was proposed to describe the hydrophobic microenvironment of CD recognition sites. The survey of CD cleavage characteristics in several proteins suggested that the HSN was a sensitive indicator for judging the favorable sites in peptides for CD cleavage, with HSN values of 0.5-1.0 representing a likely threshold. Ovalbumin (OVA), a protein resistant to CD cleavage in its native state, was easily cleaved by CD after denaturation, and the features of the cleaved peptides were quite similar to those found in BSA, where a higher HSN value indicated greater cleavability. We further conducted two-dimensional gel electrophoresis (2DE) to find more proteins that were insensitive to CD cleavage in CD-knockdown cells."
According to the news editors, the research concluded: "Based on an analysis of secondary and three-dimensional structures, we postulated that intact proteins with a structure consisting of all ?-helices would be relatively accessible to CD cleavage."
For more information on this research see: Proteolytic characteristics of cathepsin D related to the recognition and cleavage of its target proteins. Plos One, 2013;8(6):e65733. (Public Library of Science - www.plos.org; Plos One - www.plosone.org)
Our news journalists report that additional information may be obtained by contacting H. Sun, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing, People's Taiwan. Additional authors for this research include X. Lou, Q. Shan, J. Zhang, X. Zhu, J. Zhang, Y. Wang, Y. Xie, N. Xu and S. Liu (see also Enzymes and Coenzymes).
Keywords for this news article include: Asia, Beijing, Proteins, Cathepsins, Amino Acids, Peptide Hydrolases, Enzymes and Coenzymes, People's Republic of China.
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