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19 条记录 (耗时 0.031 秒)

    Purification of nucleotide sequences suitable for expression in bacteria
    5.
    发明授权
    Purification of nucleotide sequences suitable for expression in bacteria 失效
    纯化适合在细菌中表达的核苷酸序列

    公开(公告)号：US4283489A

    公开(公告)日：1981-08-11

    申请号：US97049

    申请日：1979-11-23

    申请人： Howard M. Goodman ,  John Shine ,  Peter Horst

    发明人： Howard M. Goodman ,  John Shine ,  Peter Horst

    IPC分类号： C07K14/575 ,  C12N15/10

    CPC分类号： C12N15/1003 ,  C07K14/57518 ,  C12N15/1096

    摘要： A method has been discovered for purifying a specific desired DNA sequence, starting from RNA heterogeneous in length and sequence. The steps of the method include making complementary DNA transcripts of the RNA by means of an enzyme such as reverse transcriptase, subjecting the DNA transcripts to the action of one or more selected restriction endonuclease enzymes, and fractionating the fragments produced by endonuclease action according to their length. By this method it is possible to isolate homogeneous length DNA fragments complementary to RNA sequences present in the original preparation in as low a frequency as two percent. A method is also disclosed for further purifying the homogeneous length fragments and for determining their final purity. Using the disclosed methods, a DNA fragment approximately 550 nucleotides in length coding for a portion of the peptide hormone, human chorionic somatomammotropin, has been purified to greater than 99% purity.

    摘要翻译： 已经发现了从长度和序列异质性起源的纯化特定的所需DNA序列的方法。 该方法的步骤包括通过酶如逆转录酶制备RNA的互补DNA转录物，使DNA转录物受到一种或多种选择的限制性内切核酸酶的作用，并且根据其内切核酸酶作用产生的片段进行分级 长度。 通过该方法，可以将原始制剂中存在的RNA序列互补的均质长度的DNA片段以2％的频率分离。 还公开了进一步纯化均匀长度片段并确定其最终纯度的方法。 使用所公开的方法，编码一部分肽激素（人绒毛膜促生长激素）的大约550个核苷酸长度的DNA片段已被纯化至大于99％的纯度。

    Adrenocorticotropin-lipotropin precursor gene
    7.
    发明授权
    Adrenocorticotropin-lipotropin precursor gene 失效
    促肾上腺皮质激素 - 促脂分子前体基因

    公开(公告)号：US4322499A

    公开(公告)日：1982-03-30

    申请号：US972430

    申请日：1978-12-22

    申请人： John D. Baxter ,  James L. Roberts ,  Peter H. Seeburg ,  Howard M. Goodman ,  John Shine

    发明人： John D. Baxter ,  James L. Roberts ,  Peter H. Seeburg ,  Howard M. Goodman ,  John Shine

    IPC分类号： C07K14/665 ,  C12N1/00

    CPC分类号： C07K14/665

    摘要： A technique suitable for cloning a cDNA having a base sequence coding for the ACTH/LPH precursor is disclosed. The invention is exemplified by the cloning of a cDNA fragment comprising a base sequence coding for the endorphin region. The fragment, hereinafter termed the endorphin gene cDNA sequence, was obtained from cultured mouse pituitary tumor cells known to produce the ACTH/LPH precursor protein.

    摘要翻译： 公开了一种适用于克隆编码ACTH / LPH前体碱基序列的cDNA的技术。 通过克隆包含编码内啡肽区域的碱基序列的cDNA片段来举例说明本发明。 该片段（以下称为内啡肽基因cDNA序列）从已知产生ACTH / LPH前体蛋白的培养的小鼠垂体肿瘤细胞获得。

    Fusion peptides comprising an expressible bacterial gene and .beta.-endorphin
    8.
    发明授权
    Fusion peptides comprising an expressible bacterial gene and .beta.-endorphin 失效
    融合肽包含可表达的细菌基因和β-内啡肽

    公开(公告)号：US4469631A

    公开(公告)日：1984-09-04

    申请号：US387009

    申请日：1982-06-10

    申请人： John D. Baxter ,  Ivy Fettes ,  John Shine

    发明人： John D. Baxter ,  Ivy Fettes ,  John Shine

    IPC分类号： C12N15/00 ,  C12P21/02 ,  C07C103/52 ,  C12P21/00

    CPC分类号： C12P21/02 ,  C12N15/00 ,  C12R1/19 ,  Y10S530/808

    摘要： DNA comprising the naturally occurring nucleotide sequence coding for amino acids 44-90 of .beta.-lipotropin and including the entire coding region for .beta.-endorphin with the exception of the C-terminal glutamine was modified, transferred to an expression transfer vector, and expressed as a fusion protein. The fusion protein was further modified in vitro to yield mature .beta.-endorphin. .beta.-endorphin was purified from a bacterial lysate. The structure and biological activity of the resulting product was proven by immunological assay, and by two independent assays designed to demonstrate biological activity.

    摘要翻译： 包含编码β-Lipotropin的氨基酸44-90的天然存在的核苷酸序列的DNA被修饰，转移到表达转移载体，并表达为 融合蛋白。 融合蛋白在体外进一步修饰，产生成熟的β-内啡肽。 从细菌裂解物纯化β-内啡肽。 通过免疫测定证实所得产物的结构和生物活性，并通过设计用于证明生物活性的两种独立测定来证明。