KCl-Dependent Release of Mitochondrial Membrane-Bound Arginase Appears to Be a Novel Variant of Arginase-II

Table 1

Comparative properties of Mus musculus arginase-I and arginase-II.

Parameters	Arginase-I (AAA98611.1)	Arginase-II (AAC22548.1)
Molecular weight	34807.8	38878.3
pI	6.52	6.10
Total number of negatively charged residues (Asp + Glu)	39	40
Total number of positively charged residues (Arg + Lys)	37	33
Aliphatic index	90.77	97.46
Grand average of hydropathicity (GRAVY); (http://www.expasy.org/proteomics)	−0.187	−0.109
Mitochondrial import; (https://ihg.gsf.de/ihg/mitoprot.html)	No (0.060)	Yes (0.9771)
N-phosphorylation sites; (http://www.cbs.dtu.dk/services/NetPhos/)	20 sites (9 serine residues, 6 threonine residues, and 5 tyrosine residues)	18 sites (one site S^6 (0.974) in mitochondrial targeting sequence)
N-acetylation sites; (http://www.cbs.dtu.dk/services/NetAcet/)	2 sites at 2nd S (score 0.501) and 3rd S (score 0.492) from N-terminus	No acetylation sites were found from N-terminus
O-GlcNAcetylation sites; (http://www.cbs.dtu.dk/services/YinOYang/)	9 sites	7 sites (no sites were found in mitochondrial targeting sequence)
N-glycosylation sites; (http://www.cbs.dtu.dk/services/NetNGlyc/)	5 sites	5 sites (no sites in mitochondrial targeting sequence)