A restriction enzyme from Hemophilus influenzae: II. Base sequence of the recognition site (Record no. 54834)

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control field 20250625162454.0
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Transcribing agency CICY
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Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) B-20753
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Title A restriction enzyme from Hemophilus influenzae: II. Base sequence of the recognition site
490 0# - SERIES STATEMENT
Volume/sequential designation Journal of Molecular Biology, 51(2), p.393-409, 1970
520 3# - SUMMARY, ETC.
Summary, etc. Hemophilus influenzae strain Rd contains an enzyme, endonuolease R, which specifically degrades foreign DNA. With phage T7 DNA as substrate the endonuclease introduces a limited number (about 40)double-strand breaks (5?-phosphoryl, 3?-hydroxyl). The limit product has an average length of about 1000 nucleotide pairs and contains no single-strand breaks. We have explored the nucleotide sequences at the 5?-ends of the limit product by labeling the 5?- phosphoryl groups (using polynucleotide kinase)and characterizing the labeled fragments released by various nucleases. Two classes of 5?-terminal sequences were obtained: pApApCpNp . (60 percent)and pGpApCpNp . (40 percent), where N indicates that the base in the 4th position is not unique. The dinucleoside monophosphates at the 3?-ends were isolated after micrococcal nuclease digestion of the limit product and identified as TpT(60 percent)and TpC (40 percent). We conclude that endonuclease R of H. influenzae recognizes the following specific nucleotide sequence: 5? . pGpTpPy ¦pPupApCp . 3? 3? . pCpApPup ¦PypTpGp . 5? The implications of the twofold rotational symmetry of this sequence are discussed.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Kelly Jr, T. J.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Smith, H. O.
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Uniform Resource Identifier <a href="https://drive.google.com/file/d/1F-5rnj_Lck5d8EbqYfpeTxB20srjhLo_/view?usp=drivesdk">https://drive.google.com/file/d/1F-5rnj_Lck5d8EbqYfpeTxB20srjhLo_/view?usp=drivesdk</a>
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  Clasificación local     Ref1 CICY CICY Documento préstamo interbibliotecario 25.06.2025   B-20753 25.06.2025 25.06.2025 Documentos solicitados