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1 Printed in the Republic of Korea "/"-:5*$"- 4$*&/$& 5&$)/0-0(: Vol. 25, No. 6, , Study on stability test of in process sample of recombinant Protein A Yoo Gon Kim, Woo Jong Lee, Chan Hee Won 1 and Chul Soo Shin 2 Korea Institute of Industrial Technology GyeongGi Bio-Center, 864-1, Lui-Dong, Yeongtong-Gu, Suwon-City, Gyeonggi-Do, Korea Department of Environmental Engineering, Chonbuk National University Advanced Protein Technologies(Co.) (Received September 26, 2012; Revised November 30, 2012; Accepted November 30, 2012) w " œ x w ½ š Á Á Á w», 1 w y œw 2 Advanced Protein Technologies(Co.) Abstract: This study is to investigate the issues on how to secure stability during the purification process for the production of recombinant protein A. The final recombinant protein A is produced by passing through the cation exchange column (SP) and the anion-exchange column (Q) during the production process, for which the samples produced by the step-by-step processes can be exposed to trouble in securing stable storage in case the next process cannot be taken within the proper time period. Accordingly, this study aims to evaluate the proper storage conditions and length of time when storing samples produced in the production process. That is, in this study, how to store fair samples, how long the storage period should be set up, and how to evaluate the security of its quality depending on time are dealt with. The items to be experimented with were enodotoxin, SDS-PAGE, HPLC purity and concentration. Experimental results showed that after passing the cation exchange column, when stored at 4 o C or room temperature, SDS-PAGE showed a major, endotoxin is 5.0 Eu/mg or less, and concentration is on average of 8.21 to 8.24 mg/ml and RSD% 0.10~0.62%. In addition, HLPC purity showed somewhat stable results; at the HPLC purity 214 nm, the average is 99.24% to 99.37% and RSD% is 0.22~0.29%, while the average is 89.72% to 89.80% and RSD% 0.62~1.26% at 280 nm. On the contrary, after passing the anion exchange column, when stored at 4 o C or room temperature, SDS-PAGE revealed the major, endotoxin is 0.5 Eu/mg or less, and concentration is on average of 5.59 mg/ml and RSD% 0.03~0.10%. when it comes to HLPC purity, the result showed that at the HPLC purity 214 nm, the average is 99.74% and RSD% is 0.10~0.11%, while the average is 96.16% to 96.85% and RSD% 0.72~1.13%. In conclusion, the stability of fair samples of recombinant protein A during the manufacturing process could be obtained without substance decomposition for 7~8 days at 4 o C or 20~21 days at room temperature. Corresponding author Phone : +82-(0) Fax : +82-(0)

2 484 Yoo Gon Kim, Woo Jong Lee, Chan Hee Won and Chul Soo Shin : w A w» w œ, œ ye (SP) ye (Q) mw w z w A w, œ œ ƒ w w y ƒ š. œ w š w., œ» y t sƒ w. xw m, SDS PAGE, HPLC š. x ye m z þ (4 o C), SDS PAGE major, m 5.0 Eu/mg w, s³ 8.21~8.24 mg/ml, RSD% 0.10~0.62%, š HPLC 214 nm s³ 99.24~99.37%, RSD% 0.22~0.29%, 280 nm s³ 89.72~89.80%, RSD% 0.62~1.26% ùkü. e m z þ (4 o C), SDS PAGE major, m 0.5 Eu/mg w, s³ 5.59 mg/ml, RSD% 0.03~0.10% š HPLC 214 nm s³ 99.74%, RSD% 0.10~0.11%, 280 nm s³ 96.16~96.85%, RSD% 0.72~1.13%.» x w A œ 4 C o 7~8 š 20~21 w p y. Key words: recombinant protein a, stability, endotoxin, SP, Q, HPLC x rprotein A œ x w., ye ye myw œ 4 C o y w ƒ š w, xw m, SDS PAGE, HPLC, x ww. 3FDPNCJOBOU 1SPUFJO " Protein A Staphylococcus aureus x (natural) l w wxk(recombinant)ƒ t y px w w v (Repligen) DNA sww wx 2009 ¾ y x v l w ù px ƒ š j w y wì š. wr w wì ƒ v l t yƒ 4 (USP) š. p w (monoclonal antibody) s, s ƒ w ü û w. j w ƒ w w, j w œ l j w k szw» w w ey (antibody affinity ligand) v l (protein A) w j m v(chromatography)ƒ t k š š protein A w s l w 95% ƒ ƒ wš z. w ey protein A, G, L, v l ƒƒ kv gf (Staphylococcus aureus) p mgf (Streptococcus sp.) w ey ƒ w (immunoglobulin G, IgG) v (constant region, Fc) ey ƒ v l rmpp mg f (Peptostreptococcus magnus) w eq p (kappa light chain) ey š p eq p I, III, IV w w w ƒ w scfvù Fab w r (antibody fragment) w (Fig. 1, Table 1). 1 x t t x w w t x» w w t w» w Analytical Science & Technology

3 Study on stability test of in process sample of recombinant Protein A 485 Table 2. Production process of rprotein A Fig. 1. Structure of antibody domain and affinity ligand. Table 1. Affinity ligand of monoclonal antibody used on purification Ligand Origin microbe Binding domain Protein A Staphylococcus aureus Fc region of IgG Protein G Streptococcus sp. Fc region of IgG Protein L Peptostreptococcus magnus kappa light chain of IgG š. ù t y, y, Ÿ ( ) y w, w y wš w» w w w v. w t z t w e š w ( z)» w w. t» w» w, y t sƒw x w. t x ƒ ƒ xw. š wš þ t 5±3 o C, þ t -20±5 C ³ w o š. 2-5 w " œ (E.Coli) w z w cell cell lysis w z y e (SP Column) w z y e (Q Column) z (UF) w. œ w Table 2 ù kü. 6,7 y j m v y j m v ƒ ƒƒ w w w» ƒ» w,, w. y j m v v w e ƒ w,»» ƒ. y ph j w. š yj m v y ( ) y y 2 ƒ, ƒƒ y (Na +, Cl )» w. (+) w» ( ) w ƒ ( y ) w j š, ( ) w (+) w ƒ ( y ) w k. w w j» w. ww ( ) w w l w w. 8 m ƒ w ³ m. ³ m ³ s s Vol. 25, No. 6, 2012

4 486 Yoo Gon Kim, Woo Jong Lee, Chan Hee Won and Chul Soo Shin (lipopolysaccharide) w. ³ s td w. m x ³ w m w w x, x ³ w m x y yw y j» w w. w x w» w ù. 9 x» x HPLC system Waters HPLC w, Column Phenomenex mm (BioSep- Sec-S2000) wš UV GE GeneQuant w. Endotoxin Gel Clot LONZA, Limulus Amebocyte Lysate PYROGENTPlus Single Test Kit š Electrophoresis system BIO-RAD PowerPac, Invitrogen Novexminicell & XCell SureLock w, SDS Pre made gel KOMA 4-12% Tris, KG5012 š Autopipete (20~1000 µl), Incubator, Volumetricflask, ph meter, Clean bench x» w. )1-$»» Sol. 1, 0.3 M Dibasic anhydrous sodium phosphate (21.3 g/500 ml water), Sol. 2, 0.3M Monobasic anhydrous sodium phosphate (18.0 g/500 ml water) ƒƒ Sol ml 1 L f š phƒ 7.0 ¾ Sol. 2 z 0.45 µm membrane filter w. q 214 nm, 280 nm (Mode: Dual), e L35 (BioSep-Sec-S2000), 1 ml/min, 20 µl š 20. Anhydrous sodium phosphate, Monobasic anhydrous, sodium phosphate, š Lal water w. x w A w» w e, ye (SP) m k œ 4 o C 20 ¾, 7 ¾ w Éü x ww. š ye (Q) m k œ 4 o C 21 ¾, 8 ¾ w Éü x ww. xw HPLC,, SDS Page, m 4 x w w x ww. )1-$ x x x 214 nm, 280 nm HPLC Chromatogram y w x., Chromatogram peak peakƒ % w w y wš w. š x», ye m k 4 o C xw» š w, 1, 2, 3, 6, 7, 10, 15 š 20 ƒƒ þ Éü x wwš», 1, 2, 3, 6, 7 x ww. š ye m k 4 o C», 1, 2, 3, 7, 8, 11, 15 š 21» x ww», 1, 2, 3, 7, 8 x ww. x š w A œ 1 mg/ml ( )z Blank ( )w HPLC ( : 50 µl)w 241 nm, 280 nm dual mode w. x x UV GE, GeneQuant d q 280 nm.» 5.0 mg/ml, ye»» 4 o C 20~21, 7~8 y r. w w x (USP) UV w. x 1 mg/ml ( ) z UV q 280 nm Ÿ w, 3 d w š ƒ %CV, 5% ü y w. 4%4 1"(& x x x major ƒ Á Analytical Science & Technology

5 Study on stability test of in process sample of recombinant Protein A 487 r x ye z 4 C o», 6, 10 š 20 x w w,», 3, 7 x ww. š ye z 4 C o», 3, 11, š 21,», 3 š 8 ƒƒ x ww. x» e 130V q wš Maker 15 µl gel loading z 15 µl gel loading w. Loading 50 z y w. m x x m» ye z 5.0 EU/mg w, yf z 0.5 EU/mg w. ye z 4 C o», 6, 10 š 20 x ww,», 3, 7 x ww. š ye z 4 C o», 3, 11, š 21,», 3 š 8 ƒƒ x ww. x Gel clot LONZA, Limulus Amebocyte Lysate PYROGENT Plus Single Test Kit w. x UV (mg/ml) z w Serial dilution wš 250 µl m kit w z Incubation (37 o C, 60 min) k y w. m z þ (4 o C) w y wš w. xw SDS PAGE, m, š HPLC, HPLC x 214 nm, 280 nm x ww, x»» 20 x w w. x SDS PAGE» major 20 major ùkû, m» 5.0 Eu/mg w Eu/mg w. š» 8.28 mg/ml mg/ml s³ 8.21 mg/ml, RSD% 0.1% ùkü yw ùkü. w HPLC» x 214 nm 99.12%, % 98.86~99.65% RSD% 0.29%, 280 nm» 90.58% % s³ 89.72%, RSD% 0.62% ùkü x yù w p x ye œ 41 P $ x rprotein A w» w ye Fig. 2. Result of SP sample at 4 o C storage. Table 3. Raw data of SP sample at 4 o C storage <D : Day, : Not Test> Items Time SDS PAGE <Criteria: > Endotoxin <Criteria: 5.0 EU/mg> Concentration <Criteria: 5.0 mg/ml> HPLC Purity 214 nm <Criteria: 90%> 280 nm <Criteria: 70%> Initial 1D 2D 3D 6D 7D 10D 15D 20D Vol. 25, No. 6, 2012

6 488 Yoo Gon Kim, Woo Jong Lee, Chan Hee Won and Chul Soo Shin.» x ye m z 4 o C 20 yù yw p w. Fig. 2 SP 4 o C w x š. š Table 3 x Raw data š. ye œ x ye m z w y wš w. x w SDS PAGE, m, š HPLC, HPLC x 214 nm, 280 nm x ww, x»» 7 x ww. x SDS PAGE» major 7 major ùkû, m» 5.0 Eu/mg w Eu/mg w. š» 8.28 mg/ml mg/ml s³ 8.24 mg/ml, RSD% 0.11% ùkü yw ùkü. w HPLC» x 214 nm 99.12%, % 99.12~99.71% s³ 99.37%, RSD% 0.22%, 280 nm» 90.58% % s³ 89.80%, RSD% 1.26% ùkü x yù w p.» x ye m z Fig. 3. Result of SP sample at room temperature storage. 7 yù yw p w. Fig. 3 SP 4 o C w x š. š Table 4 x Raw data š š. e œ 2 P $ x ye m z þ (4 o C) w y wš w. xw SDS PAGE, m, š HPLC, HPLC x 214 nm, 280 nm x ww, x»» 21 x ww. x SDS PAGE» major 21 major ùkû, m» 0.5 Eu/mg w Eu/mg w. š» 5.62 mg/ml mg/ml s³ 5.59 Table 4. Raw data of SP sample at room temperature storage <D : Day, : Not Test> Time Items Initial 1D 2D 3D 6D 7D SDS PAGE <Criteria: > Endotoxin <Criteria: 5.0 EU/mg> Concentration <Criteria: 5.0 mg/ml> HPLC Purity 214 nm <Criteria: 90%> 280 nm <Criteria: 70%> Analytical Science & Technology

7 Study on stability test of in process sample of recombinant Protein A 489 Fig. 4. Result of Q sample at 4 o C storage. mg/ml, RSD% 0.10% ùk ü yw ùkü. w HPLC» x 214 nm 99.55%, % 99.55~99.80% RSD% 0.10%, 280 nm» 95.84% % s³ 96.16%, RSD% 1.13% ùkü x yù w p.» x ye m z 21 yù yw p w. Fig. 4 Q 4 o C w x š. š Table 5 x Raw data š š. e œ 2 x ye m z Fig. 5. Result of Q sample at room temperature storage. w y wš w. x w SDS PAGE, m, š HPLC, HPLC x 214 nm, 280 nm x ww, x»» 8 x ww. x SDS PAGE» major 8 major ùkû, m» 0.5 Eu/mg w Eu/mg w. š» 5.62 mg/ ml mg/ml s³ 5.59 mg/ ml, RSD% 0.03% ùkü yw ùkü. w HPLC» x 214 nm 99.55%, % 95.55~99.84% RSD% 0.11%, 280 nm» 95.84% % s³ 95.91%, RSD% 0.72% ùkü x yù w p. Table 5. Raw data of Q sample at 4 o C storage <D : Day, : Not Test> Items Time SDS PAGE <Criteria: > Endotoxin <Criteria: 0.5 EU/mg> Concentration <Criteria: 5.0 mg/ml> HPLC Purity 214 nm <Criteria: 90%> 280 nm <Criteria: 70%> Initial 1D 2D 3D 7D 8D 11D 15D 21D Vol. 25, No. 6, 2012

8 490 Yoo Gon Kim, Woo Jong Lee, Chan Hee Won and Chul Soo Shin Table 6. Raw data of Q sample at room temperature storage Time HPLC Purity SDS PAGE <Criteria: > Endotoxin <Criteria: 0.5 EU/mg> Concentration <Criteria: 5.0 mg/ml> 214 nm <Criteria: 90%> 280 nm <Criteria: 70%> Items <D : Day, : Not Test> Initial 1D 2D 3D 7D 8D » x ye m z 8 yù yw p w. Fig. 5 Q 4 o C w x š. š Table 6 x Raw data š. rprotein A w» w œ q w» w x ye ye z þ (4 o C) š» þ 20~21, 7~8 w, xw SDS PAGE, m, HPLC,. ƒ œ x mw» y t s ƒ w x ye m z þ (4 o C) SDS PAGE major, m 5.0 Eu/mg w, s³ 8.21 mg/ml, RSD% 0.10% ùk ü. š HPLC» x 214 nm 99.12%, % 98.86~99.65% RSD% 0.29%, 280 nm» 90.58% % s³ 89.72%, RSD% 0.62% ùkü. ye m z x x SDS PAGE major, m 5.0 Eu/mg w, s³ 8.24 mg/ml, RSD% 0.11% ùkü š HPLC 214 nm 99.12~99.71% s³ 99.37%, RSD% 0.22%, 280 nm s³ 89.80%, RSD% 1.26% ùkü. e m z þ (4 o C) z SDS PAGE major, m 0.5 Eu/mg w,» 5.62 mg/ml mg/ml s³ 5.59 mg/ml, RSD% 0.10% š HPLC» x 214 nm 99.55%, % 99.55~99.80% RSD% 0.10%, 280 nm» 95.84% % s³ 96.16%, RSD% 1.13%. e m z x SDS PAGE major, m 0.5 Eu/mg w,» 5.62 mg/ml mg/ml s³ 5.59 mg/ml, RSD% 0.03% š HPLC» x 214 nm 95.55~ 99.84% RSD% 0.11%, 280 nm» 95.84% % s³ 95.91%, RSD% 0.72% ùkü.» x rprotein A œ (SP) þ (4 o C) 20, 7 w, w œ (Q) þ (4 o C) 21, 8 w.» w p š, y. š x 1. S. Aldington and J. Bonnerjea, Scale-up of monoclonal antibody purification processes. J. Chrom B, 848, (2007). Analytical Science & Technology

9 Study on stability test of in process sample of recombinant Protein A Guideline on Stability Testing of Biological Product - KFDA(2008). 3. ICH guideline Q5C - Quality of Biotechnological Products: Stability Testing of Biotechnological/Biological Products. 4. ICH guideline Q1A(R2) - Stability Testing of New Drug Substance and Products. 5. ICH guideline Q1E - Evaluation for Stability Data. 6. G. Strohlein, L. Aumann, T. Muller-Spath and M. Morbidelli, The multicolumn counter current solvent gradient purification process., BioPharm Int., (2007). 7. D. Agalloco, Control, et al., Process simulation testing for steril bulk pharmaceutical chemicals, PDA Technical Report No. 28, PDA J. Pharm. Sci. Technol., 52, Supplement S3 (1998). 8. S. R. Gallant, S. Vunnum and S. M. Cramer, Optimization of preparative ion-exchagen chromatography of proteins: linear gradient separations, J. Chromato A, 725, (1996). 9. S. Liu, R. Tobias and G. Jackowski, Removal of Endotoxin from Recombinant Protein Preparations, Clinical Biochem., 30(6), (1997). Vol. 25, No. 6, 2012

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