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Gene Review

SNORA44  -  small nucleolar RNA, H/ACA box 44

Homo sapiens

Synonyms: ACA44
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High impact information on SNORA44

  • Protein C inhibitor was isolated from human plasma using conventional chromatographic technique consisting of barium citrate adsorption, polyethylene glycol fractionation, DEAE-Sepharose CL-6B treatment, ammonium sulfate fractionation, dextran sulfate-agarose chromatography, gel filtration on ACA-44, and DEAE-Sephacel chromatography [1].
  • Three forms (I, IIa and IIb) of phospholipase C, hydrolyzing specifically inositol phospholipids, were resolved from human platelet cytosol and partially purified by DEAE-cellulose, phenyl-Sepharose, Ultrogel ACA-44 and hydroxylapatite column chromatographies [2].
  • The conditioned medium, containing recombinant LCAT, was harvested at 24 and 48 h and subjected to chromatography on phenyl-Sepharose and ACA-44 agarose to isolate the recombinant enzyme [3].
  • A protein extracted from a urate-calcium oxalate stone by electrodialysis is also excreted in the urine which served as the source material for its purification by FPLC after separation on an ACA44 column [4].

Analytical, diagnostic and therapeutic context of SNORA44

  • A three-step purification of (a) diafiltration and concentration, (b) column isoelectric focusing in a pH 4 to 6 gradient, and (c) ACA-44 Ultrogel column chromatography yields 25% recovery of lymphotoxin cytolytic and anticarcinogenic activities [5].


  1. Protein C inhibitor. Purification from human plasma and characterization. Suzuki, K., Nishioka, J., Hashimoto, S. J. Biol. Chem. (1983) [Pubmed]
  2. Partial purification of phosphoinositide phospholipase C from human platelet cytosol; characterization of its three forms. Banno, Y., Nakashima, S., Nozawa, Y. Biochem. Biophys. Res. Commun. (1986) [Pubmed]
  3. Purification of recombinant lecithin: cholesterol acyltransferase. Nair, M.P., Kudchodkar, B.J., Pritchard, P.H., Lacko, A.G. Protein Expr. Purif. (1997) [Pubmed]
  4. A cationic protein from a urate-calcium oxalate stone: isolation and purification of a shared protein. Binette, J.P., Binette, M.B. Scanning Microsc. (1993) [Pubmed]
  5. Molecular and biological characterization of anticarcinogenic and tumor cell growth-inhibitory activities of Syrian hamster lymphotoxin. Ransom, J.H., Evans, C.H. Cancer Res. (1983) [Pubmed]
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