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Escherichia coli Signal Peptidases Cleave the Signal Sequence of TK0522, a Carbohydrate Esterase from Hyperthermophilic Archaeon Thermococcus kodakarensis

Escherichia coli Signal Peptidases Cleave the Signal Sequence of TK0522, a Carbohydrate Esterase from Hyperthermophilic Archaeon Thermococcus kodakarensis

Anam Tariq, Alina Gul, Majida Atta Muhammad, Samia Falak and Naeem Rashid*

School of Biological Sciences, University of the Punjab, Quaid-e-Azam Campus, Lahore 54590, Pakistan

*      Corresponding author: naeem.ff.sbs @pu.edu.pk; naeemrashid37@hotmail.com

 

Fig. 1.

 Alignment of signal sequences of TK0522 from T. kodakarensis and PhoE from E. coli. Colon represent similar and asterisk show identical residues. The numbers at the right termini represent the length of the signal peptide.

Fig. 2.

Coomassie brilliant blue stained SDS-PAGE showing recombinant TK0522 in the intracellular (lanes 1–3) and extracellular (4–6) fractions. Lane M, molecular weight marker; lane 1 and 4, cells containing pET-21a(+) at 20 h post-induction; lane 2 and 5, cells containing pET-TK0522 at 4 h post-induction; lane 3 and 6, cells containing pET-TK0522 at 20 h post-induction.

Fig. 3.

Comparison of migration of intracellular and extracellular TK0522 on SDS-PAGE. Lane M, molecular weight marker; Lane 1, partially purified TK0522 in the intracellular fraction; lane 2, partially purified TK0522 in the extracellular fraction.

Pakistan Journal of Zoology

February

Vol. 52, Iss. 1, Pages 1-424

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