PURIFICATION AND ISOLATION OF ALPHA-1-PROTEINASE INHIBITOR AND DETERMINATION OF SOME OF ITS

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SAHEBGHADAM LOTFI A.; ADIBI MOTLAGH B.; MOUSAVI HOSSEINI M.K.; MAHMOUDI M.

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Journal: Pathobiology Research Year:2005 | Volume:7 | Issue:2 Page(s): 71-80

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Title

PURIFICATION AND ISOLATION OF ALPHA-1-PROTEINASE INHIBITOR AND DETERMINATION OF SOME OF ITS" PHYSICOCHEMICAL PROPERTIES

Author(s)

SAHEBGHADAM LOTFI A. | ADIBI MOTLAGH B. | MOUSAVI HOSSEINI M.K. | MAHMOUDI M. | Issue Writer Certificate

Keywords

ALPHA-I-PROTEINASE INHIBITOR (ALPHA-I-ANTITRYPSIN)Q4

PLASMA FRACTIONATIONQ3

COHN IV-I PASTEQ4

PROTEIN PURIFICATIONQ3

Abstract

Purpose: We used a method to prepare the alpha-I-proteinase inhibitor (AIPI) from the enriched Chon IV -1 paste, without complex steps and expensive chemical materials in a simple condition. The purification and isolation of the A1PI from human plasma and the determination of some of its physicochemical properties were the aims of this study. Material and Methods: Firstly, the A1PI was separated from other proteins in the IV-1 paste by two times precipitation by the polyethylene glycol. Secondly, using the ion exchange chromatography on the DEAE-Sepharose-CL6B gel the A1PI was obtained with a higher purity. The virus inactivation by the pasteurization at 60°C for 10 hours was carried out without any significant changes in the biological activity. The final product was concentrated by the ultra-filteration and lyophilized. The activity of the A1PI was determined based on its' trypsin inhibitory capacity (TIC).The single-radial immuno-diffusion (SRID) was also carried out to estimate the amount of the A1PI. Results: The results showed an AIPI purity of 0.62 with a 60 percent yield with a molecular weight determined to be about 54000 Dalton by the SDS-PAGE. For a more precise calculation of the degree of purity and confirming the antigenic property, the immuno-electrophoresis method was used against the human antiserum and the specific antiserum of the A1PI. Conclusion: Stoichiometric studies between the A1PI and trypsin showed that an amount of 1.5 to 2 µg of this protein is able to inhibit 1µg of trypsin. The inhibitory properly of the purified A1PI was comparable with the commercial product used in this regard.

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APA: Copy

SAHEBGHADAM LOTFI, A., ADIBI MOTLAGH, B., MOUSAVI HOSSEINI, M.K., & MAHMOUDI, M.. (2005). PURIFICATION AND ISOLATION OF ALPHA-1-PROTEINASE INHIBITOR AND DETERMINATION OF SOME OF ITS" PHYSICOCHEMICAL PROPERTIES . PATHOBIOLOGY RESEARCH (MODARES JOURNAL OF MEDICAL SCIENCES), 7(2), 71-80. SID. https://sid.ir/paper/81160/en

Vancouver: Copy

SAHEBGHADAM LOTFI A., ADIBI MOTLAGH B., MOUSAVI HOSSEINI M.K., MAHMOUDI M.. PURIFICATION AND ISOLATION OF ALPHA-1-PROTEINASE INHIBITOR AND DETERMINATION OF SOME OF ITS" PHYSICOCHEMICAL PROPERTIES . PATHOBIOLOGY RESEARCH (MODARES JOURNAL OF MEDICAL SCIENCES)[Internet]. 2005;7(2):71-80. Available from: https://sid.ir/paper/81160/en

IEEE: Copy

A. SAHEBGHADAM LOTFI, B. ADIBI MOTLAGH, M.K. MOUSAVI HOSSEINI, and M. MAHMOUDI, “PURIFICATION AND ISOLATION OF ALPHA-1-PROTEINASE INHIBITOR AND DETERMINATION OF SOME OF ITS" PHYSICOCHEMICAL PROPERTIES ,” PATHOBIOLOGY RESEARCH (MODARES JOURNAL OF MEDICAL SCIENCES), vol. 7, no. 2, pp. 71–80, 2005, [Online]. Available: https://sid.ir/paper/81160/en

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