Effect of partial proteolysis on the activation energy of β-N-acetylhexosaminidase precursor and mature forms

Clinical Chemistry and Laboratory Medicine

Volumn 41, Issue 3, 2003, Pages 302-305

  Hermida, Jesús ^a   Casal, J Antonio ^a   Tutor, J Carlos ^a  

^a University Hospital of Santiago de Compostela   (Spain)

Author keywords

N acetylhexosaminidase; Activation energy; Isoenzymes; Precursor and mature forms

Indexed keywords

ALBUMIN; BETA N ACETYLHEXOSAMINIDASE; ENZYME PRECURSOR; ISOENZYME; N ACETYL BETA GLUCOSAMINIDASE; PAPAIN;

ARTICLE; BLOOD ANALYSIS; CELL LYSATE; CLINICAL ARTICLE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME DEGRADATION; ENZYME SUBSTRATE; HUMAN; HYPOTHESIS; INCUBATION TIME; KIDNEY DISEASE; KIDNEY FUNCTION; LEUKOCYTE; MICROALBUMINURIA; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEINURIA; THERMODYNAMICS; THROMBOCYTE; URINALYSIS;

BETA-N-ACETYLHEXOSAMINIDASE; BLOOD PLATELETS; CASE-CONTROL STUDIES; ENZYME ACTIVATION; HUMANS; ISOENZYMES; KIDNEY DISEASES; LEUKOCYTES; PAPAIN; PEPTIDE HYDROLASES; THERMODYNAMICS;

EID: 0037256545     PISSN: 14346621     EISSN: None     Source Type: Journal    
DOI: 10.1515/CCLM.2003.048     Document Type: Article

References (23)

1. Gravel RA, Kaback MM, Proia RL, Sandhoff K, Suzuki K, Suzuki K. The GM2 gangliosidoses. In: Scriver CR, Beaudet AL, Sly WS, Valle D, editors. The metabolic and molecular bases of inherited disease. New York: McGraw-Hill, 2001: 3827-76.
2. Mahuran DJ. Biochemical consequences of mutations causing the GM2 gangliosidoses. Biochim Biophys Acta 1999; 1455:105-38.
3. Mahuran DJ, Neote K, Klavins MH, Leung A, Gravel RA. Proteolytic processing of pro-α and pro-β precursors from human β-hexosaminidase. J Biol Chem 1988; 263:4612-8.
4. Isaksson A, Hultberg B. Serum β-hexosaminidase isoenzymes are precursor forms. Scand J Clin Lab Invest 1995; 55:433-40.
5. Stein W, Bohner J, Steinhart R, Eggstein M. Macro creatine kinase: determination and differentiation of two types by their activation energies. Clin Chem 1982; 28:19-24.
6. Webers RA, Hagelauer U, Stein W, Bohner J, Faust U, Van Landeghem AAJ, et al. Indices for the age of creatine kinase M-chain in the blood. Clin Chim Acta 1985; 148:197-210.
7. Delanghe JR, De Buyzere ML, De Scheerder IK, Faust U, Wieme RJ. Activation energy and lectin affinity chromatography of gamma-glutamyltransferase as a marker for enzyme heterogeneity. Clin Biochem 1989; 22:115-9.
8. Sogo MT, Gigirey MD, Tutor JC. Activation energy of serum 5′-nucleotidase as a marker for enzyme heterogeneity. Eur J Clin Chem Clin Biochem 1994; 32:905-8.
9. Pérez LF, Gigirey D, Torío S, Tutor JC. Activation energy of serum alanyl aminopeptidase as a marker for enzyme heterogeneity in hepatobiliary disease. Clin Chem Enzym Commun 1998; 8:91-101.
10. Pérez LF, Tutor JC. Assay of β-N-acetylhexosaminidase isoenzymes in different biological specimens by means of determination of their activation energies. Clin Chem 1998; 44:226-31.
11. Pérez LF, Tutor JC. Assay of β-N-acetylhexosaminidase isoenzymes in urine by means of determination of their activation energy without removing endogenous low-molecular-mass components. Clin Chim Acta 1998; 277:39-49.
12. Pérez LF, Ribeiro HM, Casal JA, Pinto RA, Sá Miranda MC, Tutor JC. Thermodynamic characterisation of the mutated isoenzyme A of β-N-acetylhexosaminidase in GM2-gangliosidoses B1 variant. Clin Chim Acta 1999: 285:45-51.
13. Gupta GS, Raina R. Kinetics and thermodynamic transitions of N-acetyl-β-D-glucosaminidase A and B in free and bound forms: role of cellulose ion-exchanges. Mol Cell Biochem 1989; 86:65-70.
14. Pérez LF, Tutor JC. Assay of serum/plasma β-N-acetylhexosaminidase by heat inactivation using a continuous spectrophotometric method adapted to a centrifugal analyzer. Eur J Clin Chem Clin Biochem 1997; 6:445-52.
15. American Diabetes Association (ADA). Diabetic nephropathy. Diabetes Care 1997; 20 (Suppl 1):S24-S27.
16. Zühlsdorf M, Imort M, Hasilik A, Von Figura K. Molecular forms of β-hexosaminidase and cathepsin D in serum and urine of healthy subjects and patients with elevated activity of lysosomal enzymes. Biochem J 1983; 213:733-40.
17. Isaksson A, Hultberg B, Jonung T. Rat plasma clearance rate and organ distribution of β-hexosaminidase isoenzymes from human serum. Clin Chem 1992; 38:1893-98.
18. Schuette CG, Weisgerber J, Sandhoff K. Complete analysis of the glycosylation and disulfide bond pattern of human β-hexosaminidase B by MALDI-MS. Glycobiology 2001; 11:549-56.
19. Bourbouze R, Bernard M, Baumann FCh, Pérez-González N, Martín-Barrientos J, Cabezas JA. Localisation subcellulaire des isoenzymes de la N-acetyl-β-D-glucosaminidase du cortex renal de lapin. Cell Mol Biol 1984; 30:67-74.
20. Bourbouze R, Baumann FCh, Bonvalet JP, Farman N. Distribution of N-acetyl-β-D-glucosaminidase isoenzymes along the rabbit nephron. Kidney Int 1984; 25:636-42.
21. Kunin CM, Chesney RW, Graig WA, England AC, De Angelis C. Enzymuria as a marker of renal injury and disease: studies of N-acetyl-β-glucosaminidase in the general population and in patients with renal disease. Pediatrics 1978; 62:751-60.
22. Shibasaki T, Gomi H, Ishimoto F, Miyahara T. Urinary N-acetyl-β-D-glucosaminidase isoenzyme activity as measured by fast protein liquid chromatography in patients with nephrotic syndrome. Clin Chem 1990; 36:102-3.
23. Costigan MG, Rustom R, Bone JM, Shenkin A. Origin and significance of urinary N-acetyl-β-D-glucosaminidase (NAG) in renal patients with proteinuria. Clin Chim Acta 1996; 255:133-44.