Skip to main content
. 2020 Nov 18;21(22):8687. doi: 10.3390/ijms21228687

Table 4.

Good substrates, weak substrates, and products of CPZ identified using the tryptic peptide library.

Ratio CPZ/No Enzyme
Type Protein Precursor Peptide Sequence Cleaved aa Z T Obs M Theor M ppm 100 nM 10 nM 1 nM
Good Thyroglobulin GQEFTITGQKR - 2 2 1263.66 1263.60 −2 0.38 1.13 0.97
Weak Thyroglobulin ALEQATR - 2 1 787.42 787.42 3 0.57 1.04 1.00
Weak Thyroglobulin AVKQFEESQGR - 3 2 1277.64 1277.64 0 0.68 0.86 0.95
Weak Bovine serum albumin KVPQVSTPTLVEVSR - 3 2 1638.93 1638.93 −2 0.70 0.90 0.95
Weak Bovine serum albumin KQTALVELLK - 3 3 1141.69 1141.71 −22 0.73 0.80 0.89
Weak Thyroglobulin LPESK - 2 2 572.31 572.32 −24 0.77 0.83 0.83
Product Thyroglobulin GQEFTITGQK R 2 2 1107.56 1107.56 −4 1.52 0.78 1.04
Product Thyroglobulin LF R 1 1 278.16 278.15 14 1.56 0.88 0.88

Good substrates, peptides affected with a decrease ≥60% with the highest concentration of enzyme; weak substrates, peptides affected with a decrease ≥20% and <60% with the highest concentration of enzyme; Products, peptides with an increase >120% with one or more concentrations of enzyme; Cleaved aa, the amino acid cleaved by CPZ to generate the observed peptide; Z, charge; T, number of isotopic tags incorporated into each peptide; Obs M, observed monoisotopic mass; Theor M, theoretical monoisotopic mass; ppm, difference between Obs M and Theor M (in parts per million); Ratio CPZ/no enzyme, the ratio in peak intensity between the sample incubated with enzyme and the sample incubated without enzyme.