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Abi 491

Manufactured by Thermo Fisher Scientific

The ABI 491 is a laboratory instrument used for automated DNA sequencing. It is designed to perform high-throughput DNA sequencing analysis. The core function of the ABI 491 is to determine the precise order of nucleotides within DNA samples.

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4 protocols using abi 491

1

Peptide Identification and Characterization

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N-terminal sequence of the purified peptide was determined by Edman degradation on an Applied Biosystems pulsed liquid-phase sequencer (model ABI 491). Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) was used to identify the purified peptide. AXIMA CFR mass spectrometer (Kratos Analytical) was analyzed in linear and positive ion mode using an acceleration voltage of 20 kV and an accumulating time of single scanning of 50 s.
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2

Peptide Sequence Identification by MALDI-TOF

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The N-terminal sequence of the purified peptide was determined by Edman degradation on an Applied Biosystems pulsed liquid-phase sequencer (model ABI 491). Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) was used to identify the purified peptide. The AXIMA CFR mass spectrometer (Kratos Analytical) was analyzed in the linear and the positive ion mode using an acceleration voltage of 20 kV and an accumulating time of single scanning of 50 s.
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3

Peptide Sequencing and Purity Analysis

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N-terminal sequence of the purified peptide was determined by Edman degradation on an Applied Biosystems pulsed liquid-phase sequencer (model ABI 491). Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) was used to identify the purity of the isolated peptide. AXIMA CFR mass spectrometer (Kratos Analytical) was analyzed in linear and positive ion mode using an acceleration voltage of 20 kV and an accumulating time of single scanning of 50 s.
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4

Purification and Characterization of SibaCec

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According to the methods in our previous report [11 (link)], the eluted peak of A1 (Fig. 1a) containing antimicrobial activity was pooled, lyophilized, and further purified by RP-HPLC on a Wondasil C18 column (25 × 0.46 cm). The elution was performed using a linear gradient of 0–60 % acetonitrile containing 0.1 % (v/v) trifluoroacetic acid in 0.1 % (v/v) trifluoroacetic acid/water over 70 min. N-terminal sequence of the purified peptide was done by Edman degradation on an Applied Biosystems pulsed liquid-phase sequencer (model ABI 491).

Purification of SibaCec from the salivary gland of S. bannaense and MALDI–TOF MS. a The filtrate of the salivary gland homogenate of S. bannaense was divided by an Inertsil C4 RP-HPLC column. b The eluted peak of A1 containing antimicrobial activity was further purified by C18 RP-HPLC column. The purified SibaCec is indicated by an arrow. c MALDI-TOF mass spectrometry analysis of the purified SibaCec

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