N-Acetyl-b-D-Glucosaminidase

Endo G, Horiguchi S, Kiyota I. Urinary N-acetyl-B-D-glucosaminidase activity in lead-exposed workers. J AppI Toxicol 1990 10 235-238. 

N-Acetyl-B-D-glucosaminidase (N-Ac-Glu) 6 3), B-Gl ucuroni-dase (B-Glu) 4)and lactate dehydrogenase (LDH)(25lThe latter enzyme is located in the cytoplasm and is not actively secreted (as the other two enzymes are) but only set free if the cell membrane is destroyed the LDH liberated informs about viability of cell cultures or cytotoxic effects on macrophages of the substance tested. 

Lockwood TD, Bosmann FIB. The use of urinary N-acetyl-B-D-glucosaminidase in human renal toxicology I. Partial biochemical characterization and excretion in humans and release from the isolated perfused rat kidney. Toxicol AppI Pharmacol 1979 49 323-336. 

N-acetyl-B-D-glucosaminidase, alpha N-acetyl-B-D-glucosaminidase, beta N-acetyl-muramyl-L-alanine amidase Neuron-specific enolase Neutrophil-activating peptide 2 Osteocalcin Osteonectin... 

Selden A, Hultberg B, Ulander A, et al. 1993. Trichloroethylene exposure in vapour degreasing and the urinary excretion of N-acetyl-beta-D-glucosaminidase. Arch Toxicol 67 224-226. 

I. Pocsi, S. A. Taylor, A. C. Richardson, K. H. Aamlid, B. V. Smith, and R. G. Price, VRA-GlcNAc Novel substrate for N-acetyl-P-D-glucosaminidase applied to assay of this enzyme in human urine, Clin. Chem., 36 (1990) 1884-1888. 

Kitchen, B.J., Middleton, G., Salmon, M. 1978. Bovine milk N-acetyl-(3-D-glucosaminidase and its significance in the detection of abnormal udder secretions../ Dairy Res. 45, 15-20. 

Table ISA N-Acetyl-a- -D-glucosaminidase (Sanfilippo syndrome, type B, MPS 1115) ...

Enzymes. Several enzymes, for example, P-N-acetyl-D-glucosaminidase, EC 3.2.1.30 (D20), ribonuclease A, EC 3.1.27.5 (El), and the sulfliydryl protease, cathepsin B, EC 3.4.22.1 (C18), when incubated with glucose in vitro, lose considerable or all enzyme activity. The enzymes undergo nonenzymatic glycosylation resulting from the formation of reversible covalent intermediates (aldimine and ketoamine) at active-site e-amino lysines. However, the short half-life of the majority of enzymes in vivo indicates that glycosylation of cell enzymes is limited and mainly confined to the formation of reversible aldimine adducts. 

---