| Preparation of recombinant rat eosinophil-associated ribonuclease-1 and -2 and analysis of their biological activities. | |
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MedLine Citation:
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PMID: 12853122 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Rat eosinophils contain eosinophil-associated ribonucleases (Ears) in their granules. Ears are thought to be synthesized as pre-forms and stored in the granules as mature forms. However, the N-terminal amino acid of mature Ear-1 and Ear-2 is still controversial. Therefore, we prepared two recombinant mature forms of Ear-1 and Ear-2 in which the N-terminal amino acids are Ser24 (S) [Ear-1 (S) and Ear-2 (S)] and Gln26 (Q) [Ear-1 (Q) and Ear-2 (Q)], and analyzed their biological activities by comparing them with those of pre-form Ear-1 and pre-form Ear-2. The four mature Ears showed RNase A activity as well as bovine pancreatic RNase A activity, but pre-Ear-1 and pre-Ear-2 showed no RNase A activity. Mature Ear-1 (Q) and mature Ear-2 (Q) showed more potent RNase A activity than mature Ear-1 (S) and mature Ear-2 (S), respectively. The RNase A activities of mature Ear-1 (Q) and mature Ear-2 (Q) were reduced by treatment at 96 degrees C for 20 min or with RNase inhibitor. The growth of Escherichia coli was inhibited by both pre-Ears and mature Ears in a concentration-dependent manner, and was almost completely suppressed at 1.0 microM. The bactericidal activities of mature Ear-1 (Q) and mature Ear-2 (Q) were not inhibited by RNase inhibitor, but was increased by treatment at 96 degrees C for 20 min. |
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Authors:
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Kenji Ishihara; Kanako Asai; Masahiro Nakajima; Suetsugu Mue; Kazuo Ohuchi |
Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: 1638 ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 2003 Jul |
Date Detail:
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Created Date: 2003-07-10 Completed Date: 2003-08-21 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: Netherlands |
Other Details:
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Languages: eng Pagination: 164-72 Citation Subset: IM |
Affiliation:
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Laboratory of Pathophysiological Biochemistry, Graduate School of Pharmaceutical Sciences, Tohoku University, Aoba Aramaki, Aoba-ku, Sendai, Miyagi 980-8578, Japan. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals Blood Bactericidal Activity Blood Proteins Cattle Eosinophil Granule Proteins Eosinophils / enzymology, metabolism* Escherichia coli Glycine / metabolism Granulocyte-Macrophage Colony-Stimulating Factor / metabolism Hot Temperature Kinetics RNA, Transfer, Met / metabolism Rats Recombinant Proteins / chemistry, isolation & purification, metabolism* Ribonuclease, Pancreatic / blood, drug effects, genetics, metabolism Ribonucleases* Saccharomyces cerevisiae Serine / metabolism |
| Chemical | |
Reg. No./Substance:
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0/Blood Proteins; 0/Eosinophil Granule Proteins; 0/RNA, Transfer, Met; 0/Recombinant Proteins; 56-40-6/Glycine; 56-45-1/Serine; 83869-56-1/Granulocyte-Macrophage Colony-Stimulating Factor; EC 3.1.-/Ribonucleases; EC 3.1.27.5/Ribonuclease, Pancreatic |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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