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. 2018 Jul 9;9:1532. doi: 10.3389/fimmu.2018.01532

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Copyright © 2018 Anderson, Stavenhagen, Kolarich, Sommerhoff, Maurer and Metz.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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MALDI-TOF-MS analyses of whole venoms treated with purified human tryptase shows degradation of venom proteins. Venoms from five snake species [(A) common lancehead, (B) saw-scaled viper, (C) southern copperhead, (D) russel’s viper, (E), western diamondback rattlesnake] were treated with tryptase or vehicle control. Spectra were acquired within the mass range of m/z 3,500 to m/z 18,000. Samples contain equal amounts (0.5 µg) myoglobin as an internal reference (m/z 16,952 [M + H]⁺, m/z 8,476 [M + 2H]²⁺, m/z 5,651 [M + 3H]³⁺). Venom-derived signals (dashed arrows) distributed over the whole mass range were selected and normalized to the intensity of the doubly charged myoglobin signal (Figure 4B). The reduction in relative signal intensities of several peaks in tryptase-treated versus untreated venom indicates tryptase-mediated protein degradation.

MALDI-TOF-MS analyses of whole venoms treated with purified human tryptase shows degradation of venom proteins. Venoms from five snake species [(A) common lancehead, (B) saw-scaled viper, (C) southern copperhead, (D) russel’s viper, (E), western diamondback rattlesnake] were treated with tryptase or vehicle control. Spectra were acquired within the mass range of m/z 3,500 to m/z 18,000. Samples contain equal amounts (0.5 µg) myoglobin as an internal reference (m/z 16,952 [M + H]⁺, m/z 8,476 [M + 2H]²⁺, m/z 5,651 [M + 3H]³⁺). Venom-derived signals (dashed arrows) distributed over the whole mass range were selected and normalized to the intensity of the doubly charged myoglobin signal (Figure 4B). The reduction in relative signal intensities of several peaks in tryptase-treated versus untreated venom indicates tryptase-mediated protein degradation.