Addition of ATP increases the apparent molecular mass of the multicatalytic proteinase, ingensin.
A high-molecular mass ATP-dependent proteinase was shown to be identical to a multicatalytic proteinase, ingensin [(1988) Eur. J. Biochem. 177, 261-266]. The molecular mass of this proteinase increased in crude extracts of the rat liver and porcine brain, but not in the purified sample, only when the proteinase was extracted with ATP. The higher-molecular form of ingensin may be the intact one, because the concentration of ATP in vivo never decreases below 1 mM. This form of the proteinase is latent and it requires a high concentration of detergent for activation. On chromatography, it was found that the high-molecular form corresponds to the previously reported minor isoenzyme of ingensin [(1986) Biochim. Biophys. Acta 882, 297-304], ingensin A, or possibly to the ATP/ubiquitin-dependent 26S protease [(1987) J. Biol. Chem. 262, 8303-8313], and the low-molecular form to major ingensin B or the ATP/ubiquitin-independent 20 S protease.
Ishiura
S
S
National Institute of Neuroscience, NCNP, Tokyo, Japan.
Nomura
Y
Y
Tsukahara
T
T
Sugita
H
H
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001921:Brain / Q000201:enzymology; D002845:Chromatography; D002850:Chromatography, Gel; D003546:Cysteine Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D017886:Durapatite; D006882:Hydroxyapatites; D008099:Liver / Q000201:enzymology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000302:isolation & purification / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex; D011485:Protein Binding; D051381:Rats; D013379:Substrate Specificity; D013552:Swine
D006882:Hydroxyapatites; D009097:Multienzyme Complexes; D000255:Adenosine Triphosphate; D017886:Durapatite; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex