                         SEQUENCE LISTING

<110>  bioMrieux
 
<120>  Satbilisation de la GDH en solution aqueuse

<130>  STABGLU

<150>  FR13 62354
<151>  2013-12-10

<160>  3     

<170>  PatentIn version 3.5

<210>  1
<211>  421
<212>  PRT
<213>  Clostridium difficile

<400>  1

Met Ser Gly Lys Asp Val Asn Val Phe Glu Met Ala Gln Ser Gln Val 
1               5                   10                  15      


Lys Asn Ala Cys Asp Lys Leu Gly Met Glu Pro Ala Val Tyr Glu Leu 
            20                  25                  30          


Leu Lys Glu Pro Met Arg Val Ile Glu Val Ser Ile Pro Val Lys Met 
        35                  40                  45              


Asp Asp Gly Ser Ile Lys Thr Phe Lys Gly Phe Arg Ser Gln His Asn 
    50                  55                  60                  


Asp Ala Val Gly Pro Thr Lys Gly Gly Ile Arg Phe His Gln Asn Val 
65                  70                  75                  80  


Ser Arg Asp Glu Val Lys Ala Leu Ser Ile Trp Met Thr Phe Lys Cys 
                85                  90                  95      


Ser Val Thr Gly Ile Pro Tyr Gly Gly Gly Lys Gly Gly Ile Ile Val 
            100                 105                 110         


Asp Pro Ser Thr Leu Ser Gln Gly Glu Leu Glu Arg Leu Ser Arg Gly 
        115                 120                 125             


Tyr Ile Asp Gly Ile Tyr Lys Leu Ile Gly Glu Lys Val Asp Val Pro 
    130                 135                 140                 


Ala Pro Asp Val Asn Thr Asn Gly Gln Ile Met Ser Trp Met Val Asp 
145                 150                 155                 160 


Glu Tyr Asn Lys Leu Thr Gly Gln Ser Ser Ile Gly Val Ile Thr Gly 
                165                 170                 175     


Lys Pro Val Glu Phe Gly Gly Ser Leu Gly Arg Thr Ala Ala Thr Gly 
            180                 185                 190         


Phe Gly Val Ala Val Thr Ala Arg Glu Ala Ala Ala Lys Leu Gly Ile 
        195                 200                 205             


Asp Met Lys Lys Ala Lys Ile Ala Val Gln Gly Ile Gly Asn Val Gly 
    210                 215                 220                 


Ser Tyr Thr Val Leu Asn Cys Glu Lys Leu Gly Gly Thr Val Val Ala 
225                 230                 235                 240 


Met Ala Glu Trp Cys Lys Ser Glu Gly Ser Tyr Ala Ile Tyr Asn Glu 
                245                 250                 255     


Asn Gly Leu Asp Gly Gln Ala Met Leu Asp Tyr Met Lys Glu His Gly 
            260                 265                 270         


Asn Leu Leu Asn Phe Pro Gly Ala Lys Arg Ile Ser Leu Glu Glu Phe 
        275                 280                 285             


Trp Ala Ser Asp Val Asp Ile Val Ile Pro Ala Ala Leu Glu Asn Ser 
    290                 295                 300                 


Ile Thr Lys Glu Val Ala Glu Ser Ile Lys Ala Lys Leu Val Cys Glu 
305                 310                 315                 320 


Ala Ala Asn Gly Pro Thr Thr Pro Glu Ala Asp Glu Val Phe Ala Glu 
                325                 330                 335     


Arg Gly Ile Val Leu Thr Pro Asp Ile Leu Thr Asn Ala Gly Gly Val 
            340                 345                 350         


Thr Val Ser Tyr Phe Glu Trp Val Gln Asn Leu Tyr Gly Tyr Tyr Trp 
        355                 360                 365             


Ser Glu Glu Glu Val Glu Gln Lys Glu Glu Ile Ala Met Val Lys Ala 
    370                 375                 380                 


Phe Glu Ser Ile Trp Lys Ile Lys Glu Glu Tyr Asn Val Thr Met Arg 
385                 390                 395                 400 


Glu Ala Ala Tyr Met His Ser Ile Lys Lys Val Ala Glu Ala Met Lys 
                405                 410                 415     


Leu Arg Gly Trp Tyr 
            420     


<210>  2
<211>  448
<212>  PRT
<213>  Clostridium perfringens

<400>  2

Met Glu Val Lys Lys Tyr Val Asp Asn Leu Met Glu Asp Leu Lys Lys 
1               5                   10                  15      


Asn Asn Pro Gly Glu Ser Glu Phe Leu Ala Ala Ala Glu Glu Val Leu 
            20                  25                  30          


Tyr Ser Leu Val Pro Val Leu Glu Lys Asn Pro Lys Tyr Met Glu Glu 
        35                  40                  45              


Gly Ile Leu Glu Arg Ile Val Glu Pro Glu Arg Val Ile Met Phe Arg 
    50                  55                  60                  


Val Pro Trp Val Asp Asp Ala Gly Asn Val Arg Val Asn Arg Gly Tyr 
65                  70                  75                  80  


Arg Val Gln Phe Asn Ser Ala Ile Gly Pro Tyr Lys Gly Gly Leu Arg 
                85                  90                  95      


Phe His Pro Ser Val Asn Leu Ser Ile Ile Lys Phe Leu Gly Phe Glu 
            100                 105                 110         


Gln Ile Phe Lys Asn Ser Leu Thr Thr Leu Pro Ile Gly Gly Gly Lys 
        115                 120                 125             


Gly Gly Ser Asn Phe Asp Pro Lys Gly Lys Ser Asp Arg Glu Ile Met 
    130                 135                 140                 


Arg Phe Cys Gln Ser Phe Met Ser Glu Leu Tyr Arg His Ile Gly Pro 
145                 150                 155                 160 


Asn Thr Asp Val Pro Ala Gly Asp Ile Gly Val Gly Gly Arg Glu Ile 
                165                 170                 175     


Gly Tyr Met Phe Gly Gln Tyr Lys Lys Leu Lys Asn Ser Val Asp Ala 
            180                 185                 190         


Gly Val Leu Thr Gly Lys Gly Leu Thr Tyr Gly Gly Ser Leu Ala Arg 
        195                 200                 205             


Lys Glu Ala Thr Gly Tyr Gly Leu Val Tyr Phe Val Asp Glu Met Leu 
    210                 215                 220                 


Arg Asp Asn Gly Gln Thr Ile Glu Gly Lys Thr Val Val Ile Ser Gly 
225                 230                 235                 240 


Ser Gly Asn Val Ala Ile Tyr Ala Thr Glu Lys Val Gln Glu Leu Gly 
                245                 250                 255     


Gly Lys Val Val Ala Leu Ser Asp Ser Ser Gly Tyr Val Tyr Asp Glu 
            260                 265                 270         


Asn Gly Ile Asp Leu Glu Val Val Lys Glu Ile Lys Glu Val Lys Arg 
        275                 280                 285             


Gly Arg Ile Ser Glu Tyr Val Asn Tyr Val Lys Thr Ala Lys Phe Thr 
    290                 295                 300                 


Glu Gly Phe Arg Gly Ile Trp Asn Val Lys Cys Asp Ile Ala Leu Pro 
305                 310                 315                 320 


Cys Ala Thr Gln Asn Glu Ile Asp Lys Ser Ser Ala Lys Thr Leu Ile 
                325                 330                 335     


Asp Asn Gly Val Ile Ala Val Gly Glu Gly Ala Asn Met Pro Ser Thr 
            340                 345                 350         


Leu Glu Ala Gln Lys Leu Phe Val Asp Asn Lys Ile Leu Phe Ala Pro 
        355                 360                 365             


Ala Lys Ala Ala Asn Ala Gly Gly Val Ala Thr Ser Ala Leu Glu Met 
    370                 375                 380                 


Ser Gln Asn Ser Leu Arg Met Ser Trp Thr Phe Glu Glu Val Asp Ala 
385                 390                 395                 400 


Lys Leu Lys Asp Ile Met Lys Asn Ile Tyr Tyr Asn Ser Arg Asn Ala 
                405                 410                 415     


Ala Ser Glu Tyr Gly His Asp Gly Asn Leu Ile Val Gly Ala Asn Ile 
            420                 425                 430         


Ala Gly Phe Lys Lys Val Ala Asp Ala Met Leu Asp His Gly Ile Ile 
        435                 440                 445             


<210>  3
<211>  421
<212>  PRT
<213>  Clostridium botulinum

<400>  3

Met Ala Lys Glu Asn Leu Asn Pro Phe Glu Asn Ala Gln Lys Gln Val 
1               5                   10                  15      


Lys Thr Ala Cys Asp Lys Leu Gly Met Glu Pro Ala Val Tyr Glu Leu 
            20                  25                  30          


Leu Lys Glu Pro Gln Arg Val Ile Glu Val Ser Ile Pro Val Lys Met 
        35                  40                  45              


Asp Asp Gly Ser Val Lys Val Phe Lys Gly Tyr Arg Ser Gln His Asn 
    50                  55                  60                  


Asp Ala Val Gly Pro Thr Lys Gly Gly Val Arg Phe His Pro Asn Val 
65                  70                  75                  80  


Ser Leu Asp Glu Val Lys Ala Leu Ser Ile Trp Met Thr Phe Lys Cys 
                85                  90                  95      


Ser Val Thr Gly Ile Pro Tyr Gly Gly Gly Lys Gly Gly Ile Ile Val 
            100                 105                 110         


Asp Pro Lys Thr Leu Ser Lys Gly Glu Leu Glu Arg Leu Ser Arg Gly 
        115                 120                 125             


Tyr Ile Asp Gly Ile His Lys Leu Ile Gly Glu Lys Val Asp Val Pro 
    130                 135                 140                 


Ala Pro Asp Val Asn Thr Asn Gly Gln Ile Met Ala Trp Met Val Asp 
145                 150                 155                 160 


Glu Tyr Asn Lys Leu Val Gly Arg Ser Ala Ile Gly Val Ile Thr Gly 
                165                 170                 175     


Lys Pro Val Glu Phe Gly Gly Ser Leu Gly Arg Asn Ala Ala Thr Gly 
            180                 185                 190         


Phe Gly Val Ala Val Thr Ala Arg Glu Ala Ala Ala Lys Leu Gly Ile 
        195                 200                 205             


Asp Met Lys Lys Ala Lys Leu Ala Ile Gln Gly Ile Gly Asn Val Gly 
    210                 215                 220                 


Ser His Thr Val Leu Asn Cys Glu Lys Leu Gly Gly Thr Val Val Ala 
225                 230                 235                 240 


Leu Ala Glu Trp Cys Lys Glu Glu Gly Thr Tyr Ala Ile Tyr Asn Glu 
                245                 250                 255     


Asn Gly Leu Asp Gly Lys Ala Met Ile Glu Tyr Val Lys Glu Asn Gly 
            260                 265                 270         


Asn Leu Leu Gly Tyr Pro Gly Ala Lys Lys Ile Ser Leu Asp Glu Phe 
        275                 280                 285             


Trp Ala Leu Asn Val Asp Ile Leu Ile Pro Ala Ala Leu Glu Asn Ala 
    290                 295                 300                 


Ile Thr His Glu Asn Ala Ser Ser Ile Asn Ala Lys Leu Val Cys Glu 
305                 310                 315                 320 


Ala Ala Asn Gly Pro Ile Thr Pro Asp Ala Asp Ala Ile Leu Lys Glu 
                325                 330                 335     


Lys Gly Ile Thr Val Thr Pro Asp Ile Leu Thr Asn Ala Gly Gly Val 
            340                 345                 350         


Thr Val Ser Tyr Phe Glu Trp Val Gln Asn Leu Tyr Gly Tyr Tyr Trp 
        355                 360                 365             


Thr Glu Ala Glu Val Glu Ala Lys Glu Glu Glu Ala Met Val Lys Ala 
    370                 375                 380                 


Phe Glu Ser Ile Trp Ala Ile Lys Glu Glu Tyr Ser Val Thr Met Arg 
385                 390                 395                 400 


Glu Ala Ala Tyr Met His Ser Ile Lys Lys Val Ala Gly Ala Met Lys 
                405                 410                 415     


Leu Arg Gly Trp Tyr 
            420     


