Further studies on proteinases and alpha 2-macroglobulin activity in diabetic plasma.

M. Roche, T. N. Pattabiraman

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Loss of chymotrypsin binding capacity of alpha 2-macroglobulin in diabetic plasma on in vitro incubation, could be partially prevented by phenylmethyl sulphonyl fluoride and pepstatin A. Prior ten-fold dilution of plasma with 0.02 M phosphate buffer (pH 7.0) completely arrested the process. The phenomenon could not be reactivated by Ca2+, lecithin or bovine serum albumin. Diabetic plasma, like normal plasma, exhibited maximal hydrolytic activities on H-D-Pro-Phe-Arg-p-nitroanilide, H-D-Val-Leu-Arg-p-nitroanilide and H-D-Ile-Pro-Arg-p-nitroanilide. The hydrolytic activities were not significantly diminished on incubation of plasma at 37 degrees C for 12 hr, unlike alpha 2-macroglobulin activity. On gel chromatography on Sephadex G-200, part of the proteolytic activity in diabetic plasma coeluted with alpha 2-macroglobulin in the VO region. A second activity peak (absent in normal plasma) was eluted with a Ve/V0 value of 1.40. Possible role of free proteinases in diabetic plasma in the inactivation of alpha 2-macroglobulin is discussed.

Original languageEnglish
Pages (from-to)189-191
Number of pages3
JournalIndian Journal of Biochemistry and Biophysics
Volume29
Issue number2
Publication statusPublished - 01-04-1992

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alpha-Macroglobulins
Peptide Hydrolases
Plasmas
Val-Leu-Arg-p-nitroanilide
prolyl-phenylalanyl-arginine-4-nitroanilide
Lecithins
Chymotrypsin
Bovine Serum Albumin
Chromatography
Fluorides
Dilution
Gel Chromatography
Buffers
Thermodynamic properties
Gels
Phosphates

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry

Cite this

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title = "Further studies on proteinases and alpha 2-macroglobulin activity in diabetic plasma.",
abstract = "Loss of chymotrypsin binding capacity of alpha 2-macroglobulin in diabetic plasma on in vitro incubation, could be partially prevented by phenylmethyl sulphonyl fluoride and pepstatin A. Prior ten-fold dilution of plasma with 0.02 M phosphate buffer (pH 7.0) completely arrested the process. The phenomenon could not be reactivated by Ca2+, lecithin or bovine serum albumin. Diabetic plasma, like normal plasma, exhibited maximal hydrolytic activities on H-D-Pro-Phe-Arg-p-nitroanilide, H-D-Val-Leu-Arg-p-nitroanilide and H-D-Ile-Pro-Arg-p-nitroanilide. The hydrolytic activities were not significantly diminished on incubation of plasma at 37 degrees C for 12 hr, unlike alpha 2-macroglobulin activity. On gel chromatography on Sephadex G-200, part of the proteolytic activity in diabetic plasma coeluted with alpha 2-macroglobulin in the VO region. A second activity peak (absent in normal plasma) was eluted with a Ve/V0 value of 1.40. Possible role of free proteinases in diabetic plasma in the inactivation of alpha 2-macroglobulin is discussed.",
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Further studies on proteinases and alpha 2-macroglobulin activity in diabetic plasma. / Roche, M.; Pattabiraman, T. N.

In: Indian Journal of Biochemistry and Biophysics, Vol. 29, No. 2, 01.04.1992, p. 189-191.

Research output: Contribution to journalArticle

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