2002
DOI: 10.1006/prep.2001.1607
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Expression, Characterization, and Purification of Recombinant Porcine Lactoferrin in Pichia pastoris

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Cited by 44 publications
(35 citation statements)
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“…As shown in Figure 5, based on the peak heights of yeast broth and standard hLF (1.0 mg·mL −1 ), it is estimated that the concentration of expression hLF was about 1.2 mg·mL −1 , which is significantly higher than those reported by Liang and Richardson [12] and Ying et al [28]. In addition, the secretion of recombinant LF can increase by adjusting the initial pH of the culture from 6 to 7 and by the addition of ferric ions at 100 μmol·L −1 to the medium [25].…”
Section: Optimization Of Hlf Expressionmentioning
confidence: 73%
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“…As shown in Figure 5, based on the peak heights of yeast broth and standard hLF (1.0 mg·mL −1 ), it is estimated that the concentration of expression hLF was about 1.2 mg·mL −1 , which is significantly higher than those reported by Liang and Richardson [12] and Ying et al [28]. In addition, the secretion of recombinant LF can increase by adjusting the initial pH of the culture from 6 to 7 and by the addition of ferric ions at 100 μmol·L −1 to the medium [25].…”
Section: Optimization Of Hlf Expressionmentioning
confidence: 73%
“…The Pichia pastoris system has now been used successfully to express a large number of intracellular and secreted proteins. Extremely high levels have been obtained for some biologically active molecules [6], and LF has been shown to be expressed in P. pastoris with the highest yield of 115 mg·L −1 [17,18,25,28]. In this paper, the effect of the ratio of glycerol and methanol on the expression of hLF and the growth of yeast cells were determined by dot blotting and OD600.…”
Section: Optimization Of Hlf Expressionmentioning
confidence: 99%
“…Each lobe binds one Fe 3+ ion. In some cases the expression levels of hLF have been influenced by supplementation of FeCl 3 [36]. In order to identify the optimal concentration of FeCl 3 , the induction medium was supplemented with FeCl 3 in the range of 0.05-2.0 mM final concentration.…”
Section: Optimization Of Recombinant Human Lactoferrin Expression In mentioning
confidence: 99%
“…[15][16][17] Previous reports have demonstrated that functional proteins of N-half molecule (N-lobe) of human serum transferrin and ovotransferrin can be produced in microorganisms (Pichia pastoris and Escherichia coli, respectively). [18][19][20] Although the P. pastoris expression system of the whole molecule of porcine lactoferrin and equine lactoferrin have been developed recently, 21,22) the microorganism production system of whole molecule of Fe 3þ -transporter proteins, such as serum transferrin and ovotransferrin has not been available.…”
mentioning
confidence: 99%