Score: 4.00 | Title: An active DNA transposon family in rice .
| Author: Jiang N Bao Z Zhang X Hirochika H Eddy SR McCouch SR Wessler SR .
| Journal: Nature Citation: V : 421 ( 6919 ) P : 163-7 Year: 2003 | Literature: oryza Field: abstract Doc ID: pub12520302 | Abstract: The publication of draft sequences for the two subspecies of Oryza sativa ( rice ) , japonica ( cv .
Nipponbare ) and indica ( cv .
93-11 ) , provides a unique opportunity to study the dynamics of transposable elements in this important crop plant .
Here we report the use of these sequences in a computational approach to identify the first active DNA transposons from rice and the first active miniature inverted-repeat transposable element ( MITE ) from any organism .
A sequence classified as a Tourist-like MITE of 430 base pairs , called miniature Ping ( mPing ) , was present in about 70 copies in Nipponbare and in about 14 copies in 93-11 .
These mPing elements , which are all nearly identical , transpose actively in an indica cell-culture line .
Database searches identified a family of related transposase-encoding elements ( called Pong ) , which also transpose actively in the same cells .
Virtually all new insertions of mPing and Pong elements were into low-copy regions of the rice genome .
Since the domestication of rice mPing MITEs have been amplified preferentially in cultivars adapted to environmental extremes-a situation that is reminiscent of the genomic shock theory for transposon activation . | Matching Sentences: [ Sen. 5, subscore: 1.00 ]: The publication of draft sequences for the two subspecies of Oryza sativa ( rice ) , japonica ( cv . Nipponbare ) and indica ( cv . 93-11 ) , provides a unique opportunity to study the dynamics of transposable elements in this important crop plant . Here we report the use of these sequences in a computational approach to identify the first active DNA transposons from rice and the first active miniature inverted-repeat transposable element ( MITE ) from any organism . A sequence classified as a Tourist-like MITE of 430 base pairs , called miniature Ping ( mPing ) , was present in about 70 copies in Nipponbare and in about 14 copies in 93-11 . These mPing elements , which are all nearly identical , transpose actively in an indica cell-culture line . Database searches identified a family of related transposase-encoding elements ( called Pong ) , which also transpose actively in the same cells . Virtually all new insertions of mPing and Pong elements were into low-copy regions of the rice genome . Since the domestication of rice mPing MITEs have been amplified preferentially in cultivars adapted to environmental extremes-a situation that is reminiscent of the genomic shock theory for transposon activation . [ Sen. 6, subscore: 1.00 ]: The publication of draft sequences for the two subspecies of Oryza sativa ( rice ) , japonica ( cv . Nipponbare ) and indica ( cv . 93-11 ) , provides a unique opportunity to study the dynamics of transposable elements in this important crop plant . Here we report the use of these sequences in a computational approach to identify the first active DNA transposons from rice and the first active miniature inverted-repeat transposable element ( MITE ) from any organism . A sequence classified as a Tourist-like MITE of 430 base pairs , called miniature Ping ( mPing ) , was present in about 70 copies in Nipponbare and in about 14 copies in 93-11 . These mPing elements , which are all nearly identical , transpose actively in an indica cell-culture line . Database searches identified a family of related transposase-encoding elements ( called Pong ) , which also transpose actively in the same cells . Virtually all new insertions of mPing and Pong elements were into low-copy regions of the rice genome . Since the domestication of rice mPing MITEs have been amplified preferentially in cultivars adapted to environmental extremes-a situation that is reminiscent of the genomic shock theory for transposon activation . [ Sen. 8, subscore: 1.00 ]: The publication of draft sequences for the two subspecies of Oryza sativa ( rice ) , japonica ( cv . Nipponbare ) and indica ( cv . 93-11 ) , provides a unique opportunity to study the dynamics of transposable elements in this important crop plant . Here we report the use of these sequences in a computational approach to identify the first active DNA transposons from rice and the first active miniature inverted-repeat transposable element ( MITE ) from any organism . A sequence classified as a Tourist-like MITE of 430 base pairs , called miniature Ping ( mPing ) , was present in about 70 copies in Nipponbare and in about 14 copies in 93-11 . These mPing elements , which are all nearly identical , transpose actively in an indica cell-culture line . Database searches identified a family of related transposase-encoding elements ( called Pong ) , which also transpose actively in the same cells . Virtually all new insertions of mPing and Pong elements were into low-copy regions of the rice genome . Since the domestication of rice mPing MITEs have been amplified preferentially in cultivars adapted to environmental extremes-a situation that is reminiscent of the genomic shock theory for transposon activation . [ Sen. 9, subscore: 1.00 ]: The publication of draft sequences for the two subspecies of Oryza sativa ( rice ) , japonica ( cv . Nipponbare ) and indica ( cv . 93-11 ) , provides a unique opportunity to study the dynamics of transposable elements in this important crop plant . Here we report the use of these sequences in a computational approach to identify the first active DNA transposons from rice and the first active miniature inverted-repeat transposable element ( MITE ) from any organism . A sequence classified as a Tourist-like MITE of 430 base pairs , called miniature Ping ( mPing ) , was present in about 70 copies in Nipponbare and in about 14 copies in 93-11 . These mPing elements , which are all nearly identical , transpose actively in an indica cell-culture line . Database searches identified a family of related transposase-encoding elements ( called Pong ) , which also transpose actively in the same cells . Virtually all new insertions of mPing and Pong elements were into low-copy regions of the rice genome . Since the domestication of rice mPing MITEs have been amplified preferentially in cultivars adapted to environmental extremes-a situation that is reminiscent of the genomic shock theory for transposon activation .
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Score: 15.00 | Title: Purification and characterization of a high molecular mass serine carboxypeptidase from Monascus pilosus .
| Author: Liu F Tachibana S Taira T Ishihara M Kato F Yasuda M | Journal: J Ind . Microbiol . Biotechnol . Citation: V : 31 ( 12 ) P : 572-80 Year: 2004 | Literature: oryza Field: abstract Doc ID: pub15592905 | Abstract: Two serine carboxypeptidases , MpiCP-1 and MpiCP-2 , were purified to homogeneity from Monascus pilosus IFO 4480 .
MpiCP-1 is a homodimer with a native molecular mass of 125 kDa composed of two identical subunits of 61 kDa , while MpiCP-2 is a high mass homooligomer with a native molecular mass of 2 , 263 kDa composed of about 38 identical subunits of 59 kDa .
This is unique among carboxypeptidases and distinguishes MpiCP-2 as the largest known carboxypeptidase .
The two purified enzymes were both acidic glycoproteins .
MpiCP-1 has an isoelectric point of 3 . 7 and a carbohydrate content of 11% , while for MpiCP-2 these values were 4 . 0 and 33% , respectively .
The optimum pH and temperature were around 4 . 0 and 50 degrees C for MpiCP-1 , and 3 . 5 and 50 degrees C for MpiCP-2 .
MpiCP-1 was stable over a broad range of pH between 2 . 0 and 8 . 0 at 37 degrees C for 1 h , and up to 55 degrees C for 15 min at pH 6 . 0 , but MpiCP-2 was stable in a narrow range of pH between 5 . 5 and 6 . 5 , and up to 50 degrees C for 15 min at pH 6 . 0 .
Phenylmethylsulfonylfluoride strongly inhibited MpiCP-1 and completely inhibited MpiCP-2 , suggesting that they are both serine carboxypeptidases .
Of the substrates tested , benzyloxycarbonyl-L : -tyrosyl-L : -glutamic acid ( Z-Tyr-Glu ) was the best for both enzymes .
The Km , Vmax , Kcat and Kcat/Km values of MpiCP-1 for Z-Tyr-Glu at pH 4 . 0 and 37 degrees C were 1 . 33 mM , 1 . 49 mM min ( -1 ) , 723 s ( -1 ) and 545 mM ( -1 ) s ( -1 ) , and those of MpiCP-2 at pH 3 . 5 and 37 degrees C were 1 . 55 mM , 1 . 54 mM min ( -1 ) , 2 , 039 s ( -1 ) and 1 , 318 mM ( -1 ) s ( -1 ) , respectively . | Matching Sentences: [ Sen. 1, subscore: 2.00 ]: Two serine carboxypeptidases , MpiCP-1 and MpiCP-2 , were purified to homogeneity from Monascus pilosus IFO 4480 . MpiCP-1 is a homodimer with a native molecular mass of 125 kDa composed of two identical subunits of 61 kDa , while MpiCP-2 is a high mass homooligomer with a native molecular mass of 2 , 263 kDa composed of about 38 identical subunits of 59 kDa . This is unique among carboxypeptidases and distinguishes MpiCP-2 as the largest known carboxypeptidase . The two purified enzymes were both acidic glycoproteins . MpiCP-1 has an isoelectric point of 3 . 7 and a carbohydrate content of 11% , while for MpiCP-2 these values were 4 . 0 and 33% , respectively . The optimum pH and temperature were around 4 . 0 and 50 degrees C for MpiCP-1 , and 3 . 5 and 50 degrees C for MpiCP-2 . MpiCP-1 was stable over a broad range of pH between 2 . 0 and 8 . 0 at 37 degrees C for 1 h , and up to 55 degrees C for 15 min at pH 6 . 0 , but MpiCP-2 was stable in a narrow range of pH between 5 . 5 and 6 . 5 , and up to 50 degrees C for 15 min at pH 6 . 0 . Phenylmethylsulfonylfluoride strongly inhibited MpiCP-1 and completely inhibited MpiCP-2 , suggesting that they are both serine carboxypeptidases . Of the substrates tested , benzyloxycarbonyl-L : -tyrosyl-L : -glutamic acid ( Z-Tyr-Glu ) was the best for both enzymes . The Km , Vmax , Kcat and Kcat/Km values of MpiCP-1 for Z-Tyr-Glu at pH 4 . 0 and 37 degrees C were 1 . 33 mM , 1 . 49 mM min ( -1 ) , 723 s ( -1 ) and 545 mM ( -1 ) s ( -1 ) , and those of MpiCP-2 at pH 3 . 5 and 37 degrees C were 1 . 55 mM , 1 . 54 mM min ( -1 ) , 2 , 039 s ( -1 ) and 1 , 318 mM ( -1 ) s ( -1 ) , respectively . [ Sen. 2, subscore: 2.00 ]: Two serine carboxypeptidases , MpiCP-1 and MpiCP-2 , were purified to homogeneity from Monascus pilosus IFO 4480 . MpiCP-1 is a homodimer with a native molecular mass of 125 kDa composed of two identical subunits of 61 kDa , while MpiCP-2 is a high mass homooligomer with a native molecular mass of 2 , 263 kDa composed of about 38 identical subunits of 59 kDa . This is unique among carboxypeptidases and distinguishes MpiCP-2 as the largest known carboxypeptidase . The two purified enzymes were both acidic glycoproteins . MpiCP-1 has an isoelectric point of 3 . 7 and a carbohydrate content of 11% , while for MpiCP-2 these values were 4 . 0 and 33% , respectively . The optimum pH and temperature were around 4 . 0 and 50 degrees C for MpiCP-1 , and 3 . 5 and 50 degrees C for MpiCP-2 . MpiCP-1 was stable over a broad range of pH between 2 . 0 and 8 . 0 at 37 degrees C for 1 h , and up to 55 degrees C for 15 min at pH 6 . 0 , but MpiCP-2 was stable in a narrow range of pH between 5 . 5 and 6 . 5 , and up to 50 degrees C for 15 min at pH 6 . 0 . Phenylmethylsulfonylfluoride strongly inhibited MpiCP-1 and completely inhibited MpiCP-2 , suggesting that they are both serine carboxypeptidases . Of the substrates tested , benzyloxycarbonyl-L : -tyrosyl-L : -glutamic acid ( Z-Tyr-Glu ) was the best for both enzymes . The Km , Vmax , Kcat and Kcat/Km values of MpiCP-1 for Z-Tyr-Glu at pH 4 . 0 and 37 degrees C were 1 . 33 mM , 1 . 49 mM min ( -1 ) , 723 s ( -1 ) and 545 mM ( -1 ) s ( -1 ) , and those of MpiCP-2 at pH 3 . 5 and 37 degrees C were 1 . 55 mM , 1 . 54 mM min ( -1 ) , 2 , 039 s ( -1 ) and 1 , 318 mM ( -1 ) s ( -1 ) , respectively . [ Sen. 5, subscore: 2.00 ]: Two serine carboxypeptidases , MpiCP-1 and MpiCP-2 , were purified to homogeneity from Monascus pilosus IFO 4480 . MpiCP-1 is a homodimer with a native molecular mass of 125 kDa composed of two identical subunits of 61 kDa , while MpiCP-2 is a high mass homooligomer with a native molecular mass of 2 , 263 kDa composed of about 38 identical subunits of 59 kDa . This is unique among carboxypeptidases and distinguishes MpiCP-2 as the largest known carboxypeptidase . The two purified enzymes were both acidic glycoproteins . MpiCP-1 has an isoelectric point of 3 . 7 and a carbohydrate content of 11% , while for MpiCP-2 these values were 4 . 0 and 33% , respectively . The optimum pH and temperature were around 4 . 0 and 50 degrees C for MpiCP-1 , and 3 . 5 and 50 degrees C for MpiCP-2 . MpiCP-1 was stable over a broad range of pH between 2 . 0 and 8 . 0 at 37 degrees C for 1 h , and up to 55 degrees C for 15 min at pH 6 . 0 , but MpiCP-2 was stable in a narrow range of pH between 5 . 5 and 6 . 5 , and up to 50 degrees C for 15 min at pH 6 . 0 . Phenylmethylsulfonylfluoride strongly inhibited MpiCP-1 and completely inhibited MpiCP-2 , suggesting that they are both serine carboxypeptidases . Of the substrates tested , benzyloxycarbonyl-L : -tyrosyl-L : -glutamic acid ( Z-Tyr-Glu ) was the best for both enzymes . The Km , Vmax , Kcat and Kcat/Km values of MpiCP-1 for Z-Tyr-Glu at pH 4 . 0 and 37 degrees C were 1 . 33 mM , 1 . 49 mM min ( -1 ) , 723 s ( -1 ) and 545 mM ( -1 ) s ( -1 ) , and those of MpiCP-2 at pH 3 . 5 and 37 degrees C were 1 . 55 mM , 1 . 54 mM min ( -1 ) , 2 , 039 s ( -1 ) and 1 , 318 mM ( -1 ) s ( -1 ) , respectively . [ Sen. 6, subscore: 2.00 ]: Two serine carboxypeptidases , MpiCP-1 and MpiCP-2 , were purified to homogeneity from Monascus pilosus IFO 4480 . MpiCP-1 is a homodimer with a native molecular mass of 125 kDa composed of two identical subunits of 61 kDa , while MpiCP-2 is a high mass homooligomer with a native molecular mass of 2 , 263 kDa composed of about 38 identical subunits of 59 kDa . This is unique among carboxypeptidases and distinguishes MpiCP-2 as the largest known carboxypeptidase . The two purified enzymes were both acidic glycoproteins . MpiCP-1 has an isoelectric point of 3 . 7 and a carbohydrate content of 11% , while for MpiCP-2 these values were 4 . 0 and 33% , respectively . The optimum pH and temperature were around 4 . 0 and 50 degrees C for MpiCP-1 , and 3 . 5 and 50 degrees C for MpiCP-2 . MpiCP-1 was stable over a broad range of pH between 2 . 0 and 8 . 0 at 37 degrees C for 1 h , and up to 55 degrees C for 15 min at pH 6 . 0 , but MpiCP-2 was stable in a narrow range of pH between 5 . 5 and 6 . 5 , and up to 50 degrees C for 15 min at pH 6 . 0 . Phenylmethylsulfonylfluoride strongly inhibited MpiCP-1 and completely inhibited MpiCP-2 , suggesting that they are both serine carboxypeptidases . Of the substrates tested , benzyloxycarbonyl-L : -tyrosyl-L : -glutamic acid ( Z-Tyr-Glu ) was the best for both enzymes . The Km , Vmax , Kcat and Kcat/Km values of MpiCP-1 for Z-Tyr-Glu at pH 4 . 0 and 37 degrees C were 1 . 33 mM , 1 . 49 mM min ( -1 ) , 723 s ( -1 ) and 545 mM ( -1 ) s ( -1 ) , and those of MpiCP-2 at pH 3 . 5 and 37 degrees C were 1 . 55 mM , 1 . 54 mM min ( -1 ) , 2 , 039 s ( -1 ) and 1 , 318 mM ( -1 ) s ( -1 ) , respectively . [ Sen. 7, subscore: 2.00 ]: Two serine carboxypeptidases , MpiCP-1 and MpiCP-2 , were purified to homogeneity from Monascus pilosus IFO 4480 . MpiCP-1 is a homodimer with a native molecular mass of 125 kDa composed of two identical subunits of 61 kDa , while MpiCP-2 is a high mass homooligomer with a native molecular mass of 2 , 263 kDa composed of about 38 identical subunits of 59 kDa . This is unique among carboxypeptidases and distinguishes MpiCP-2 as the largest known carboxypeptidase . The two purified enzymes were both acidic glycoproteins . MpiCP-1 has an isoelectric point of 3 . 7 and a carbohydrate content of 11% , while for MpiCP-2 these values were 4 . 0 and 33% , respectively . The optimum pH and temperature were around 4 . 0 and 50 degrees C for MpiCP-1 , and 3 . 5 and 50 degrees C for MpiCP-2 . MpiCP-1 was stable over a broad range of pH between 2 . 0 and 8 . 0 at 37 degrees C for 1 h , and up to 55 degrees C for 15 min at pH 6 . 0 , but MpiCP-2 was stable in a narrow range of pH between 5 . 5 and 6 . 5 , and up to 50 degrees C for 15 min at pH 6 . 0 . Phenylmethylsulfonylfluoride strongly inhibited MpiCP-1 and completely inhibited MpiCP-2 , suggesting that they are both serine carboxypeptidases . Of the substrates tested , benzyloxycarbonyl-L : -tyrosyl-L : -glutamic acid ( Z-Tyr-Glu ) was the best for both enzymes . The Km , Vmax , Kcat and Kcat/Km values of MpiCP-1 for Z-Tyr-Glu at pH 4 . 0 and 37 degrees C were 1 . 33 mM , 1 . 49 mM min ( -1 ) , 723 s ( -1 ) and 545 mM ( -1 ) s ( -1 ) , and those of MpiCP-2 at pH 3 . 5 and 37 degrees C were 1 . 55 mM , 1 . 54 mM min ( -1 ) , 2 , 039 s ( -1 ) and 1 , 318 mM ( -1 ) s ( -1 ) , respectively . [ Sen. 8, subscore: 2.00 ]: Two serine carboxypeptidases , MpiCP-1 and MpiCP-2 , were purified to homogeneity from Monascus pilosus IFO 4480 . MpiCP-1 is a homodimer with a native molecular mass of 125 kDa composed of two identical subunits of 61 kDa , while MpiCP-2 is a high mass homooligomer with a native molecular mass of 2 , 263 kDa composed of about 38 identical subunits of 59 kDa . This is unique among carboxypeptidases and distinguishes MpiCP-2 as the largest known carboxypeptidase . The two purified enzymes were both acidic glycoproteins . MpiCP-1 has an isoelectric point of 3 . 7 and a carbohydrate content of 11% , while for MpiCP-2 these values were 4 . 0 and 33% , respectively . The optimum pH and temperature were around 4 . 0 and 50 degrees C for MpiCP-1 , and 3 . 5 and 50 degrees C for MpiCP-2 . MpiCP-1 was stable over a broad range of pH between 2 . 0 and 8 . 0 at 37 degrees C for 1 h , and up to 55 degrees C for 15 min at pH 6 . 0 , but MpiCP-2 was stable in a narrow range of pH between 5 . 5 and 6 . 5 , and up to 50 degrees C for 15 min at pH 6 . 0 . Phenylmethylsulfonylfluoride strongly inhibited MpiCP-1 and completely inhibited MpiCP-2 , suggesting that they are both serine carboxypeptidases . Of the substrates tested , benzyloxycarbonyl-L : -tyrosyl-L : -glutamic acid ( Z-Tyr-Glu ) was the best for both enzymes . The Km , Vmax , Kcat and Kcat/Km values of MpiCP-1 for Z-Tyr-Glu at pH 4 . 0 and 37 degrees C were 1 . 33 mM , 1 . 49 mM min ( -1 ) , 723 s ( -1 ) and 545 mM ( -1 ) s ( -1 ) , and those of MpiCP-2 at pH 3 . 5 and 37 degrees C were 1 . 55 mM , 1 . 54 mM min ( -1 ) , 2 , 039 s ( -1 ) and 1 , 318 mM ( -1 ) s ( -1 ) , respectively . [ Sen. 10, subscore: 2.00 ]: Two serine carboxypeptidases , MpiCP-1 and MpiCP-2 , were purified to homogeneity from Monascus pilosus IFO 4480 . MpiCP-1 is a homodimer with a native molecular mass of 125 kDa composed of two identical subunits of 61 kDa , while MpiCP-2 is a high mass homooligomer with a native molecular mass of 2 , 263 kDa composed of about 38 identical subunits of 59 kDa . This is unique among carboxypeptidases and distinguishes MpiCP-2 as the largest known carboxypeptidase . The two purified enzymes were both acidic glycoproteins . MpiCP-1 has an isoelectric point of 3 . 7 and a carbohydrate content of 11% , while for MpiCP-2 these values were 4 . 0 and 33% , respectively . The optimum pH and temperature were around 4 . 0 and 50 degrees C for MpiCP-1 , and 3 . 5 and 50 degrees C for MpiCP-2 . MpiCP-1 was stable over a broad range of pH between 2 . 0 and 8 . 0 at 37 degrees C for 1 h , and up to 55 degrees C for 15 min at pH 6 . 0 , but MpiCP-2 was stable in a narrow range of pH between 5 . 5 and 6 . 5 , and up to 50 degrees C for 15 min at pH 6 . 0 . Phenylmethylsulfonylfluoride strongly inhibited MpiCP-1 and completely inhibited MpiCP-2 , suggesting that they are both serine carboxypeptidases . Of the substrates tested , benzyloxycarbonyl-L : -tyrosyl-L : -glutamic acid ( Z-Tyr-Glu ) was the best for both enzymes . The Km , Vmax , Kcat and Kcat/Km values of MpiCP-1 for Z-Tyr-Glu at pH 4 . 0 and 37 degrees C were 1 . 33 mM , 1 . 49 mM min ( -1 ) , 723 s ( -1 ) and 545 mM ( -1 ) s ( -1 ) , and those of MpiCP-2 at pH 3 . 5 and 37 degrees C were 1 . 55 mM , 1 . 54 mM min ( -1 ) , 2 , 039 s ( -1 ) and 1 , 318 mM ( -1 ) s ( -1 ) , respectively . [ Sen. 3, subscore: 1.00 ]: Two serine carboxypeptidases , MpiCP-1 and MpiCP-2 , were purified to homogeneity from Monascus pilosus IFO 4480 . MpiCP-1 is a homodimer with a native molecular mass of 125 kDa composed of two identical subunits of 61 kDa , while MpiCP-2 is a high mass homooligomer with a native molecular mass of 2 , 263 kDa composed of about 38 identical subunits of 59 kDa . This is unique among carboxypeptidases and distinguishes MpiCP-2 as the largest known carboxypeptidase . The two purified enzymes were both acidic glycoproteins . MpiCP-1 has an isoelectric point of 3 . 7 and a carbohydrate content of 11% , while for MpiCP-2 these values were 4 . 0 and 33% , respectively . The optimum pH and temperature were around 4 . 0 and 50 degrees C for MpiCP-1 , and 3 . 5 and 50 degrees C for MpiCP-2 . MpiCP-1 was stable over a broad range of pH between 2 . 0 and 8 . 0 at 37 degrees C for 1 h , and up to 55 degrees C for 15 min at pH 6 . 0 , but MpiCP-2 was stable in a narrow range of pH between 5 . 5 and 6 . 5 , and up to 50 degrees C for 15 min at pH 6 . 0 . Phenylmethylsulfonylfluoride strongly inhibited MpiCP-1 and completely inhibited MpiCP-2 , suggesting that they are both serine carboxypeptidases . Of the substrates tested , benzyloxycarbonyl-L : -tyrosyl-L : -glutamic acid ( Z-Tyr-Glu ) was the best for both enzymes . The Km , Vmax , Kcat and Kcat/Km values of MpiCP-1 for Z-Tyr-Glu at pH 4 . 0 and 37 degrees C were 1 . 33 mM , 1 . 49 mM min ( -1 ) , 723 s ( -1 ) and 545 mM ( -1 ) s ( -1 ) , and those of MpiCP-2 at pH 3 . 5 and 37 degrees C were 1 . 55 mM , 1 . 54 mM min ( -1 ) , 2 , 039 s ( -1 ) and 1 , 318 mM ( -1 ) s ( -1 ) , respectively .
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