Expression of tuna growth hormone cDNA in Escherichia coli

Summary In order to produce tuna (Thunnus thynnus) growth hormone (GH), expression plasmid (pUES13S) carrying tuna GH cDNA was constructed using a vector (pKK223-3), in which the replication origin was replaced with that of pUC19. The expression of the tuna GH cDNA was greatly affected by the distan...
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Autor*in:	Sato, Nobuyuki [verfasserIn] Hayami, Tsuyoshi Murata, Kousaku Watanabe, Kunihiko Kariya, Yutaka Sakaguchi, Morihiko Kimura, Shoji Nonaka, Michio Kimura, Akira

Format:	Artikel
Sprache:	Englisch

Erschienen:	1989

Schlagwörter:	Escherichia Coli Western Blot Codon Blot Analysis Growth Hormone

Anmerkung:	© Springer-Verlag 1989

Übergeordnetes Werk:	Enthalten in: Applied microbiology and biotechnology - Springer-Verlag, 1984, 30(1989), 2 vom: Feb., Seite 153-159
Übergeordnetes Werk:	volume:30 ; year:1989 ; number:2 ; month:02 ; pages:153-159

Links:	Volltext

DOI / URN:	10.1007/BF00264004

Katalog-ID:	OLC2050655509

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520			\|a Summary In order to produce tuna (Thunnus thynnus) growth hormone (GH), expression plasmid (pUES13S) carrying tuna GH cDNA was constructed using a vector (pKK223-3), in which the replication origin was replaced with that of pUC19. The expression of the tuna GH cDNA was greatly affected by the distance between a Shine-Dalgarno (SD) sequence and the initiation codon (ATG) and was most efficient when the distance was adjusted to 13 base pairs (bp). The amount of tuna GH produced by Escherichia coli JM109 with pUES13S was more than 12.5% of the total cytosolic proteins and the product was immunologically identified to be tuna GH (mol. wt. 21 000) by Western blot analysis using tuna GH specific immunoglobulin G (IgG). Another plasmid (pUES13S-2) containing tandemly polymerized tuna GH cDNA was constructed, to improve the productivity of tuna GH. When E. coli JM109 carrying pUES13S-2 was incubated at 40°C, the amount of tuna GH produced reached about 20% of the total cytosolic proteins.
650		4	\|a Escherichia Coli
650		4	\|a Western Blot
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650		4	\|a Growth Hormone
700	1		\|a Hayami, Tsuyoshi \|4 aut
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700	1		\|a Watanabe, Kunihiko \|4 aut
700	1		\|a Kariya, Yutaka \|4 aut
700	1		\|a Sakaguchi, Morihiko \|4 aut
700	1		\|a Kimura, Shoji \|4 aut
700	1		\|a Nonaka, Michio \|4 aut
700	1		\|a Kimura, Akira \|4 aut
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allfields	10.1007/BF00264004 doi (DE-627)OLC2050655509 (DE-He213)BF00264004-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Sato, Nobuyuki verfasserin aut Expression of tuna growth hormone cDNA in Escherichia coli 1989 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1989 Summary In order to produce tuna (Thunnus thynnus) growth hormone (GH), expression plasmid (pUES13S) carrying tuna GH cDNA was constructed using a vector (pKK223-3), in which the replication origin was replaced with that of pUC19. The expression of the tuna GH cDNA was greatly affected by the distance between a Shine-Dalgarno (SD) sequence and the initiation codon (ATG) and was most efficient when the distance was adjusted to 13 base pairs (bp). The amount of tuna GH produced by Escherichia coli JM109 with pUES13S was more than 12.5% of the total cytosolic proteins and the product was immunologically identified to be tuna GH (mol. wt. 21 000) by Western blot analysis using tuna GH specific immunoglobulin G (IgG). Another plasmid (pUES13S-2) containing tandemly polymerized tuna GH cDNA was constructed, to improve the productivity of tuna GH. When E. coli JM109 carrying pUES13S-2 was incubated at 40°C, the amount of tuna GH produced reached about 20% of the total cytosolic proteins. Escherichia Coli Western Blot Codon Blot Analysis Growth Hormone Hayami, Tsuyoshi aut Murata, Kousaku aut Watanabe, Kunihiko aut Kariya, Yutaka aut Sakaguchi, Morihiko aut Kimura, Shoji aut Nonaka, Michio aut Kimura, Akira aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 30(1989), 2 vom: Feb., Seite 153-159 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:30 year:1989 number:2 month:02 pages:153-159 https://doi.org/10.1007/BF00264004 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2006 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4028 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4219 GBV_ILN_4302 GBV_ILN_4307 GBV_ILN_4310 AR 30 1989 2 02 153-159
spelling	10.1007/BF00264004 doi (DE-627)OLC2050655509 (DE-He213)BF00264004-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Sato, Nobuyuki verfasserin aut Expression of tuna growth hormone cDNA in Escherichia coli 1989 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1989 Summary In order to produce tuna (Thunnus thynnus) growth hormone (GH), expression plasmid (pUES13S) carrying tuna GH cDNA was constructed using a vector (pKK223-3), in which the replication origin was replaced with that of pUC19. The expression of the tuna GH cDNA was greatly affected by the distance between a Shine-Dalgarno (SD) sequence and the initiation codon (ATG) and was most efficient when the distance was adjusted to 13 base pairs (bp). The amount of tuna GH produced by Escherichia coli JM109 with pUES13S was more than 12.5% of the total cytosolic proteins and the product was immunologically identified to be tuna GH (mol. wt. 21 000) by Western blot analysis using tuna GH specific immunoglobulin G (IgG). Another plasmid (pUES13S-2) containing tandemly polymerized tuna GH cDNA was constructed, to improve the productivity of tuna GH. When E. coli JM109 carrying pUES13S-2 was incubated at 40°C, the amount of tuna GH produced reached about 20% of the total cytosolic proteins. Escherichia Coli Western Blot Codon Blot Analysis Growth Hormone Hayami, Tsuyoshi aut Murata, Kousaku aut Watanabe, Kunihiko aut Kariya, Yutaka aut Sakaguchi, Morihiko aut Kimura, Shoji aut Nonaka, Michio aut Kimura, Akira aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 30(1989), 2 vom: Feb., Seite 153-159 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:30 year:1989 number:2 month:02 pages:153-159 https://doi.org/10.1007/BF00264004 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2006 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4028 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4219 GBV_ILN_4302 GBV_ILN_4307 GBV_ILN_4310 AR 30 1989 2 02 153-159
allfields_unstemmed	10.1007/BF00264004 doi (DE-627)OLC2050655509 (DE-He213)BF00264004-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Sato, Nobuyuki verfasserin aut Expression of tuna growth hormone cDNA in Escherichia coli 1989 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1989 Summary In order to produce tuna (Thunnus thynnus) growth hormone (GH), expression plasmid (pUES13S) carrying tuna GH cDNA was constructed using a vector (pKK223-3), in which the replication origin was replaced with that of pUC19. The expression of the tuna GH cDNA was greatly affected by the distance between a Shine-Dalgarno (SD) sequence and the initiation codon (ATG) and was most efficient when the distance was adjusted to 13 base pairs (bp). The amount of tuna GH produced by Escherichia coli JM109 with pUES13S was more than 12.5% of the total cytosolic proteins and the product was immunologically identified to be tuna GH (mol. wt. 21 000) by Western blot analysis using tuna GH specific immunoglobulin G (IgG). Another plasmid (pUES13S-2) containing tandemly polymerized tuna GH cDNA was constructed, to improve the productivity of tuna GH. When E. coli JM109 carrying pUES13S-2 was incubated at 40°C, the amount of tuna GH produced reached about 20% of the total cytosolic proteins. Escherichia Coli Western Blot Codon Blot Analysis Growth Hormone Hayami, Tsuyoshi aut Murata, Kousaku aut Watanabe, Kunihiko aut Kariya, Yutaka aut Sakaguchi, Morihiko aut Kimura, Shoji aut Nonaka, Michio aut Kimura, Akira aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 30(1989), 2 vom: Feb., Seite 153-159 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:30 year:1989 number:2 month:02 pages:153-159 https://doi.org/10.1007/BF00264004 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2006 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4028 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4219 GBV_ILN_4302 GBV_ILN_4307 GBV_ILN_4310 AR 30 1989 2 02 153-159
allfieldsGer	10.1007/BF00264004 doi (DE-627)OLC2050655509 (DE-He213)BF00264004-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Sato, Nobuyuki verfasserin aut Expression of tuna growth hormone cDNA in Escherichia coli 1989 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1989 Summary In order to produce tuna (Thunnus thynnus) growth hormone (GH), expression plasmid (pUES13S) carrying tuna GH cDNA was constructed using a vector (pKK223-3), in which the replication origin was replaced with that of pUC19. The expression of the tuna GH cDNA was greatly affected by the distance between a Shine-Dalgarno (SD) sequence and the initiation codon (ATG) and was most efficient when the distance was adjusted to 13 base pairs (bp). The amount of tuna GH produced by Escherichia coli JM109 with pUES13S was more than 12.5% of the total cytosolic proteins and the product was immunologically identified to be tuna GH (mol. wt. 21 000) by Western blot analysis using tuna GH specific immunoglobulin G (IgG). Another plasmid (pUES13S-2) containing tandemly polymerized tuna GH cDNA was constructed, to improve the productivity of tuna GH. When E. coli JM109 carrying pUES13S-2 was incubated at 40°C, the amount of tuna GH produced reached about 20% of the total cytosolic proteins. Escherichia Coli Western Blot Codon Blot Analysis Growth Hormone Hayami, Tsuyoshi aut Murata, Kousaku aut Watanabe, Kunihiko aut Kariya, Yutaka aut Sakaguchi, Morihiko aut Kimura, Shoji aut Nonaka, Michio aut Kimura, Akira aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 30(1989), 2 vom: Feb., Seite 153-159 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:30 year:1989 number:2 month:02 pages:153-159 https://doi.org/10.1007/BF00264004 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2006 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4028 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4219 GBV_ILN_4302 GBV_ILN_4307 GBV_ILN_4310 AR 30 1989 2 02 153-159
allfieldsSound	10.1007/BF00264004 doi (DE-627)OLC2050655509 (DE-He213)BF00264004-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Sato, Nobuyuki verfasserin aut Expression of tuna growth hormone cDNA in Escherichia coli 1989 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1989 Summary In order to produce tuna (Thunnus thynnus) growth hormone (GH), expression plasmid (pUES13S) carrying tuna GH cDNA was constructed using a vector (pKK223-3), in which the replication origin was replaced with that of pUC19. The expression of the tuna GH cDNA was greatly affected by the distance between a Shine-Dalgarno (SD) sequence and the initiation codon (ATG) and was most efficient when the distance was adjusted to 13 base pairs (bp). The amount of tuna GH produced by Escherichia coli JM109 with pUES13S was more than 12.5% of the total cytosolic proteins and the product was immunologically identified to be tuna GH (mol. wt. 21 000) by Western blot analysis using tuna GH specific immunoglobulin G (IgG). Another plasmid (pUES13S-2) containing tandemly polymerized tuna GH cDNA was constructed, to improve the productivity of tuna GH. When E. coli JM109 carrying pUES13S-2 was incubated at 40°C, the amount of tuna GH produced reached about 20% of the total cytosolic proteins. Escherichia Coli Western Blot Codon Blot Analysis Growth Hormone Hayami, Tsuyoshi aut Murata, Kousaku aut Watanabe, Kunihiko aut Kariya, Yutaka aut Sakaguchi, Morihiko aut Kimura, Shoji aut Nonaka, Michio aut Kimura, Akira aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 30(1989), 2 vom: Feb., Seite 153-159 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:30 year:1989 number:2 month:02 pages:153-159 https://doi.org/10.1007/BF00264004 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2006 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4028 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4219 GBV_ILN_4302 GBV_ILN_4307 GBV_ILN_4310 AR 30 1989 2 02 153-159
language	English
source	Enthalten in Applied microbiology and biotechnology 30(1989), 2 vom: Feb., Seite 153-159 volume:30 year:1989 number:2 month:02 pages:153-159
sourceStr	Enthalten in Applied microbiology and biotechnology 30(1989), 2 vom: Feb., Seite 153-159 volume:30 year:1989 number:2 month:02 pages:153-159
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Escherichia Coli Western Blot Codon Blot Analysis Growth Hormone
dewey-raw	570
isfreeaccess_bool	false
container_title	Applied microbiology and biotechnology
authorswithroles_txt_mv	Sato, Nobuyuki @@aut@@ Hayami, Tsuyoshi @@aut@@ Murata, Kousaku @@aut@@ Watanabe, Kunihiko @@aut@@ Kariya, Yutaka @@aut@@ Sakaguchi, Morihiko @@aut@@ Kimura, Shoji @@aut@@ Nonaka, Michio @@aut@@ Kimura, Akira @@aut@@
publishDateDaySort_date	1989-02-01T00:00:00Z
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author	Sato, Nobuyuki
spellingShingle	Sato, Nobuyuki ddc 570 ssgn 12 fid BIODIV misc Escherichia Coli misc Western Blot misc Codon misc Blot Analysis misc Growth Hormone Expression of tuna growth hormone cDNA in Escherichia coli
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topic_title	570 VZ 12 ssgn BIODIV DE-30 fid Expression of tuna growth hormone cDNA in Escherichia coli Escherichia Coli Western Blot Codon Blot Analysis Growth Hormone
topic	ddc 570 ssgn 12 fid BIODIV misc Escherichia Coli misc Western Blot misc Codon misc Blot Analysis misc Growth Hormone
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title	Expression of tuna growth hormone cDNA in Escherichia coli
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title_full	Expression of tuna growth hormone cDNA in Escherichia coli
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author_browse	Sato, Nobuyuki Hayami, Tsuyoshi Murata, Kousaku Watanabe, Kunihiko Kariya, Yutaka Sakaguchi, Morihiko Kimura, Shoji Nonaka, Michio Kimura, Akira
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title_sort	expression of tuna growth hormone cdna in escherichia coli
title_auth	Expression of tuna growth hormone cDNA in Escherichia coli
abstract	Summary In order to produce tuna (Thunnus thynnus) growth hormone (GH), expression plasmid (pUES13S) carrying tuna GH cDNA was constructed using a vector (pKK223-3), in which the replication origin was replaced with that of pUC19. The expression of the tuna GH cDNA was greatly affected by the distance between a Shine-Dalgarno (SD) sequence and the initiation codon (ATG) and was most efficient when the distance was adjusted to 13 base pairs (bp). The amount of tuna GH produced by Escherichia coli JM109 with pUES13S was more than 12.5% of the total cytosolic proteins and the product was immunologically identified to be tuna GH (mol. wt. 21 000) by Western blot analysis using tuna GH specific immunoglobulin G (IgG). Another plasmid (pUES13S-2) containing tandemly polymerized tuna GH cDNA was constructed, to improve the productivity of tuna GH. When E. coli JM109 carrying pUES13S-2 was incubated at 40°C, the amount of tuna GH produced reached about 20% of the total cytosolic proteins. © Springer-Verlag 1989
abstractGer	Summary In order to produce tuna (Thunnus thynnus) growth hormone (GH), expression plasmid (pUES13S) carrying tuna GH cDNA was constructed using a vector (pKK223-3), in which the replication origin was replaced with that of pUC19. The expression of the tuna GH cDNA was greatly affected by the distance between a Shine-Dalgarno (SD) sequence and the initiation codon (ATG) and was most efficient when the distance was adjusted to 13 base pairs (bp). The amount of tuna GH produced by Escherichia coli JM109 with pUES13S was more than 12.5% of the total cytosolic proteins and the product was immunologically identified to be tuna GH (mol. wt. 21 000) by Western blot analysis using tuna GH specific immunoglobulin G (IgG). Another plasmid (pUES13S-2) containing tandemly polymerized tuna GH cDNA was constructed, to improve the productivity of tuna GH. When E. coli JM109 carrying pUES13S-2 was incubated at 40°C, the amount of tuna GH produced reached about 20% of the total cytosolic proteins. © Springer-Verlag 1989
abstract_unstemmed	Summary In order to produce tuna (Thunnus thynnus) growth hormone (GH), expression plasmid (pUES13S) carrying tuna GH cDNA was constructed using a vector (pKK223-3), in which the replication origin was replaced with that of pUC19. The expression of the tuna GH cDNA was greatly affected by the distance between a Shine-Dalgarno (SD) sequence and the initiation codon (ATG) and was most efficient when the distance was adjusted to 13 base pairs (bp). The amount of tuna GH produced by Escherichia coli JM109 with pUES13S was more than 12.5% of the total cytosolic proteins and the product was immunologically identified to be tuna GH (mol. wt. 21 000) by Western blot analysis using tuna GH specific immunoglobulin G (IgG). Another plasmid (pUES13S-2) containing tandemly polymerized tuna GH cDNA was constructed, to improve the productivity of tuna GH. When E. coli JM109 carrying pUES13S-2 was incubated at 40°C, the amount of tuna GH produced reached about 20% of the total cytosolic proteins. © Springer-Verlag 1989
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title_short	Expression of tuna growth hormone cDNA in Escherichia coli
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author2	Hayami, Tsuyoshi Murata, Kousaku Watanabe, Kunihiko Kariya, Yutaka Sakaguchi, Morihiko Kimura, Shoji Nonaka, Michio Kimura, Akira
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