Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Blanca Lain"'
Autor:
Gregory Zarbis-Papastoitsis, Emily Belcher Schirmer, Michael Christopher Kuczewski, Blanca Lain
Publikováno v:
Biotechnology Journal. 6:56-65
Advances in single-use technologies can enable greater speed, flexibility, and a smaller footprint for multi-product production facilities, such as at a contract manufacturer. Recent efforts in the area of cell line and media optimization have result
Publikováno v:
Journal of Biological Chemistry. 273:4406-4415
Of the two homologous isozymes of aspartate aminotransferase that are also nearly identical in their folded structures, only the mitochondrial form (mAAT) is synthesized as a precursor (pmAAT). After its in vitro synthesis in rabbit reticulocyte lysa
Publikováno v:
Journal of Biological Chemistry. 270:24732-24739
The precursor (pmAspAT) and mature (mAspAT) forms of mitochondrial aspartate aminotransferase interact with hsp70 very early during translation when synthesized in either rabbit reticulocyte lysate or wheat germ extract (Lain, B., Iriarte, A., and Ma
Autor:
Carol Zehetmeier, Bradley T. Scroggins, Christine Margarete Unger, Leodevico L. Ilag, Len Neckers, Claudia Torella, Daniel G. Jay, Dean Yimlamai, Brenda K. Eustace, Jean K. Stewart, Blanca Lain, Gerald Beste, Stefan W. Henning, Takashi Sakurai
Publikováno v:
Nature cell biology. 6(6)
Tumour cell invasiveness is crucial for cancer metastasis and is not yet understood. Here we describe two functional screens for proteins required for the invasion of fibrosarcoma cells that identified the molecular chaperone heat shock protein 90 (h
Publikováno v:
Biochemistry and Molecular Biology of Vitamin B6 and PQQ-dependent Proteins ISBN: 9783034895491
To investigate the possible interaction of mitochondrial aspartate aminotransferase (mAAT) with cytosolic components, a photoreactive probe was incorporated co-translationally into mAAT chains synthesized in a cell-free extract. Irradiation of the tr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8310111f743bdc7d0d00a9bd3fb9930a
https://doi.org/10.1007/978-3-0348-8397-9_40
https://doi.org/10.1007/978-3-0348-8397-9_40
Publikováno v:
The Journal of biological chemistry. 269(22)
The precursor to mitochondrial aspartate amino-transferase (pmAspAT), when newly synthesized in vitro using either rabbit reticulocyte lysate (RRL) or wheat germ extract (WGE), is highly susceptible to proteolysis. Treatment of these translation prod
Publikováno v:
European journal of biochemistry. 202(3)
An enzyme which catalyzes the transamination of L-alanine with 2-oxoglutarate has been purified 157-fold to electrophoretic homogeneity from the unicellular green alga Chlamydomonas reinhardtii 6145c. The enzyme showed maximal activity at pH 7.3 and
Publikováno v:
Physiologia Plantarum. 74:433-439
The isolation and characterization of an l-aspartate aminotransferase (AAT) activity (EC 2.6.1.1) in the unicellular green alga Chlamydomonas reinhardtii 6145c are reported for the first time. The enzyme transaminates aspartate with the 2-oxoglutarat