Article(id=1279144433719423989, tenantId=1146029695717560320, journalId=1279045329999892481, issueId=1279144148057960780, articleNumber=PA20260323_LxOeCHrJ, orderNo=null, doi=10.19556/j.0258-7033.20241219-03, pmid=null, cstr=null, oa=null, hot=0, price=null, onlineType=0, articleFormat=0, articleType=null, articleTypeStr=null, receivedDate=null, receivedDateStr=null, revisedDate=null, revisedDateStr=null, acceptedDate=null, acceptedDateStr=null, onlineDate=1782901398353, onlineDateStr=2026-07-01, pubDate=1765814400000, pubDateStr=2025-12-16, doiRegisterDate=null, doiRegisterDateStr=null, onlineIssueDate=1782901398353, onlineIssueDateStr=2026-07-01, onlineJustAcceptDate=null, onlineJustAcceptDateStr=null, onlineFirstDate=null, onlineFirstDateStr=null, sourceXml=null, magXml=null, createTime=1782901398353, creator=admin, updateTime=1782901398353, updator=admin, issue=Issue{id=1279144148057960780, tenantId=1146029695717560320, journalId=1279045329999892481, year='2026', volume='62', 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tenantId=1146029695717560320, journalId=1279045329999892481, language=CN, title=武定鸡FABP6基因克隆及生物信息学分析, columnId=1282278076700660488, journalTitle=中国畜牧杂志, columnName=畜牧生物技术, runingTitle=null, highlight=null, articleAbstract=本研究旨在克隆武定鸡脂肪酸结合蛋白6(FABP6)基因CDS区序列并进行生物信息学分析,为后续研究FABP6基因对武定鸡脂肪代谢与沉积的影响提供参考。以武定鸡为试验对象,设计FABP6引物、提取总RNA、反转录、PCR扩增并克隆其编码区序列,并进行同源性比对及系统进化树构建;运用生物信息学软件对其编码蛋白的理化性质、亲/疏水性、跨膜区、信号肽、修饰结构、保守结构域及二、三级结构进行预测。结果显示:武定鸡FABP6基因CDS序列全长387 bp,FABP6蛋白等电点7.82,平均疏水指数-0.566,为亲水蛋白,不存在信号肽和跨膜区,主要定位于细胞质。FABP6蛋白被14个磷酸化位点修饰,无糖基化位点,主要由α-螺旋、延伸链和无规卷曲构成。武定鸡FABP6与原鸡、火鸡、珍珠鸡、雪鸡、环颈雉鸡、鹌鹑、鸿雁、棕硬尾鸭、天鹅和绿头鸭基因同源性分别为99.2%、96.6%、96.4%、96.1%、96.1%、95.9%、90.2%、89.7%、89.7%和89.4%。FABP6蛋白与FABP2、FABP3、FABP4、FABP5、FABP7、FABP9、NR1H4、RXRA、SLC10A2和SNX24蛋白存在互作关系。本研究明确了FABP6基因在武定鸡脂肪代谢与沉积中的核心作用,为其分子机制的深入解析奠定了理论基础,也为我国优质地方鸡种的肉质改良与高效新品种培育提供了候选基因。, authors=邱文才1 , 苏航1 , 杨明华1 , 赵素梅1 , 潘洪彬1 , 黄英1 , 李永能2 , authorsList=邱文才, 苏航, 杨明华, 赵素梅, 潘洪彬, 黄英, 李永能, authorCompany=1.云南农业大学动物科学技术学院,云南省动物营养与饲料重点实验室; 2.云南农业大学组织部,动物医学院, correspAuthors=黄英, authorNote=邱文才,男,云南昆明人,硕士,主要从事动物营养与饲料科学研究,E-mail:qiuqiudx@163.com;, correspAuthorsNote=null, copyrightStatement=null, copyrightOwner=null, extLink=null, articleAbsUrl=null, sourceXml=null, magXml=null, pdfUrl=null, pdf=b5fHZWig2WR7HWKGp7A5gw==, pdfFileSize=2429231, pdfExtLink=null, richHtmlUrl=null, mobilePdfUrl=null, reviewReport=null, pdfFirstPage=null, abstractGraph=null, abstractGraphContent=null, abstractVideo=null, citation=null, cebUrl=null, magXmlContent=null, mapNumber=null, fund=国家十四五重点研发计划项目(2022YFD1601905);)}, authors=[Author(id=1288197464314319128, tenantId=1146029695717560320, journalId=null, articleId=1279144433719423989, orderNo=null, firstName=null, middleName=null, lastName=null, nameCn=null, orcid=null, stid=null, country=null, authorPic=null, dead=null, email=null, emailSecond=null, emailThird=null, correspondingAuthor=null, authorType=null, ext={CN=AuthorExt(id=null, tenantId=null, journalId=1279045329999892481, articleId=1279144433719423989, 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Structural and dynamic roles of permanent water molecules in ligand molecular recognition by chicken liver bile acid binding protein[J]. J Mol Recognit, 2010, 21(5):348-354. [17]Eliseo T, Ragona L, Catalano M, et al. Structural and dynamic determinants of ligand binding in the ternary complex of chicken liver bile acid binding protein with two bile salts revealed by NMR[J]. FEBS J, 2007, 283(3):541-555. [18]Nolan V, Perduca M, Monaco H L, et al. Chicken liver bile acid-binding protein is in a compact partly folded state at acidic pH. Its relevance to the interaction with lipid membranes[J].Biochemistry, 2005, 44(23):8486-8493. [19]Nichesola D, Perduca M, Capaldi S, et al. Crystal structure of chicken liver basic fatty acid-binding protein complexed with cholic acid[J]. Biochemistry, 2004, 43(44):14072-14079. [20]Tsai I T, Wu C C, Hung W C, et al. FABP1 and FABP2 as markers of diabetic nephropathy[J]. Int J Med Sci, 2020,17(15):2338-2345. [21]Zhang X, Tang B C, Li J M, et al. Comparative transcriptome analysis reveals mechanisms of restriction feeding on lipid metabolism in ducks[J]. Poult Sci, 2023, 102(10):102963. [22]Young A C, Scapin G, Kromminga A, et al. Structural studies on human muscle fatty acid binding protein at 1.4 A resolution:binding interactions with three C18 fatty acids[J]. Structure,1994, 2(6):523-534. [23]梁前进,王鹏程,白燕荣.蛋白质磷酸化修饰研究进展[J].科技导报, 2012, 30(31):73-79. [24]Sacchettini J C, Gordon J I, Banaszak L J. Crystal structure of rat intestinal fatty acid binding protein:refinement and analysis of the Escherichia coli derived protein with bound palmitate[J].J Mol Biol, 1989, 208(2):327-339. [25]Lassen D, Lücke C, Kveder M, et al. Three-dimensional structure of bovine heart fatty acid-binding protein with boundpalmitic acid, determined by multidimensional NMR spectroscopy[J]. Eur J Biochem, 1995, 230:266-280. [26]Balendiran G K, Schnütgen F, Scapin G, et al. Crystal structure and thermodynamic analysis of human brain fatty acid-binding protein[J]. J Biol Chem, 2000, 275:27045-27054. [27]Lücke C, Rademacher M, Zimmerman A W, et al. Spin-system heterogeneities indicate a selected-fit mechanism in fatty acid binding to heart-type fatty acid-binding protein(H-FABP)[J].Biochem J, 2001, 354:259-266. [28]石鹏飞,许家利,孙金魁,许厚强.关岭牛FABP1和FABP2基因克隆及其组织表达分析[J].南方农业学报, 2023, 54(2):598-608. [29]Masato F, Shigeyuki S, Kazuaki S, et al. Fatty acid binding protein 4(FABP4):Pathophysiological insightsand potent clinical biomarker of metabolic and cardiovascular diseases[J].Clin Med Insights Cardiol, 2014, 8(S3):23-33. [30]Ardicli S, Samli H, Alpay F, et al. Association of single nucleotide polymorphisms in the FABP4 gene with carcass characteristics and meat quality in Holstein bulls[J]. Ann Anim Sci, 2017, 17(1):117-130. [31]Niewold T A, Meinen M, Vand M J. Plasma intestinal fatty acid binding protein(I-FABP)concentrations increase following intestinal ischemia in pigs[J]. Res Vet Sci, 2004, 77(1):89-91. [32]王卓.延边牛FABP5、FABP6、DGAT1、USP43、P2RY10和FUBP3多态性与生长性状关联分析[D].延吉:延边大学,2023. [33]Michal J J, Zhang Z W, Gaskins C T, et al. The bovine fatty acid binding protein 4 gene is significantly associated with marbling and subcutaneous fat depth in Wagyu×Limousin F2crosses[J]. Anim Genet, 2006, 37(4):400-402. [34]Shin S C, Heo J P, Chung E R. Genetic variants of the FABP4gene are associated with marbling scores and meat quality grades in Hanwoo(Korean cattle)[J]. Mol Biol Rep, 2012,39(5):5323-5330. [35]Gerbens F, Verburg F J, Van Moerkerk H T, et al. Associations of heart and adipocyte fatty acid-binding protein gene expression with intramuscular fat content in pigs[J]. J Anim Sci,2001, 79(2):347-354. [36]廖秀冬,任立明,王光瑛,李昂,黄银花.北京鸭FABP2基因多态性与体尺和屠体性状的相关性研究[J].中国家禽,2012, 34(17):23-26. [37]徐松松,安荣荣,陈耀峰,程敏,李辉,王守志.鸡FABP2基因单倍型与生长和体组成性状的相关分析[J].中国家禽,2016, 38(8):5-9.)
中国畜牧杂志
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武定鸡FABP6基因克隆及生物信息学分析
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邱文才, 苏航, 杨明华, 赵素梅, 潘洪彬, 黄英, 李永能
作者信息
作者简介:
邱文才,男,云南昆明人,硕士,主要从事动物营养与饲料科学研究,E-mail:qiuqiudx@163.com;
Affiliations
出版时间: 2025-12-16
doi: 10.19556/j.0258-7033.20241219-03
文章导航
本研究旨在克隆武定鸡脂肪酸结合蛋白6(FABP6)基因CDS区序列并进行生物信息学分析,为后续研究FABP6基因对武定鸡脂肪代谢与沉积的影响提供参考。以武定鸡为试验对象,设计FABP6引物、提取总RNA、反转录、PCR扩增并克隆其编码区序列,并进行同源性比对及系统进化树构建;运用生物信息学软件对其编码蛋白的理化性质、亲/疏水性、跨膜区、信号肽、修饰结构、保守结构域及二、三级结构进行预测。结果显示:武定鸡FABP6基因CDS序列全长387 bp,FABP6蛋白等电点7.82,平均疏水指数-0.566,为亲水蛋白,不存在信号肽和跨膜区,主要定位于细胞质。FABP6蛋白被14个磷酸化位点修饰,无糖基化位点,主要由α-螺旋、延伸链和无规卷曲构成。武定鸡FABP6与原鸡、火鸡、珍珠鸡、雪鸡、环颈雉鸡、鹌鹑、鸿雁、棕硬尾鸭、天鹅和绿头鸭基因同源性分别为99.2%、96.6%、96.4%、96.1%、96.1%、95.9%、90.2%、89.7%、89.7%和89.4%。FABP6蛋白与FABP2、FABP3、FABP4、FABP5、FABP7、FABP9、NR1H4、RXRA、SLC10A2和SNX24蛋白存在互作关系。本研究明确了FABP6基因在武定鸡脂肪代谢与沉积中的核心作用,为其分子机制的深入解析奠定了理论基础,也为我国优质地方鸡种的肉质改良与高效新品种培育提供了候选基因。
武定鸡
/
FABP6基因
/
基因克隆
/
生物信息学分析
邱文才, 苏航, 杨明华, 赵素梅, 潘洪彬, 黄英, 李永能.
武定鸡FABP6基因克隆及生物信息学分析.
中国畜牧杂志,
2026
, 62
(2)
: 345
-353
.
DOI: 10.19556/j.0258-7033.20241219-03
参考文献
引证文献
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Structural and dynamic roles of permanent water molecules in ligand molecular recognition by chicken liver bile acid binding protein[J]. J Mol Recognit, 2010, 21(5):348-354. [17]Eliseo T, Ragona L, Catalano M, et al. Structural and dynamic determinants of ligand binding in the ternary complex of chicken liver bile acid binding protein with two bile salts revealed by NMR[J]. FEBS J, 2007, 283(3):541-555. [18]Nolan V, Perduca M, Monaco H L, et al. Chicken liver bile acid-binding protein is in a compact partly folded state at acidic pH. Its relevance to the interaction with lipid membranes[J].Biochemistry, 2005, 44(23):8486-8493. [19]Nichesola D, Perduca M, Capaldi S, et al. Crystal structure of chicken liver basic fatty acid-binding protein complexed with cholic acid[J]. Biochemistry, 2004, 43(44):14072-14079. [20]Tsai I T, Wu C C, Hung W C, et al. FABP1 and FABP2 as markers of diabetic nephropathy[J]. Int J Med Sci, 2020,17(15):2338-2345. [21]Zhang X, Tang B C, Li J M, et al. Comparative transcriptome analysis reveals mechanisms of restriction feeding on lipid metabolism in ducks[J]. Poult Sci, 2023, 102(10):102963. [22]Young A C, Scapin G, Kromminga A, et al. Structural studies on human muscle fatty acid binding protein at 1.4 A resolution:binding interactions with three C18 fatty acids[J]. Structure,1994, 2(6):523-534. [23]梁前进,王鹏程,白燕荣.蛋白质磷酸化修饰研究进展[J].科技导报, 2012, 30(31):73-79. [24]Sacchettini J C, Gordon J I, Banaszak L J. Crystal structure of rat intestinal fatty acid binding protein:refinement and analysis of the Escherichia coli derived protein with bound palmitate[J].J Mol Biol, 1989, 208(2):327-339. [25]Lassen D, Lücke C, Kveder M, et al. Three-dimensional structure of bovine heart fatty acid-binding protein with boundpalmitic acid, determined by multidimensional NMR spectroscopy[J]. Eur J Biochem, 1995, 230:266-280. [26]Balendiran G K, Schnütgen F, Scapin G, et al. Crystal structure and thermodynamic analysis of human brain fatty acid-binding protein[J]. J Biol Chem, 2000, 275:27045-27054. [27]Lücke C, Rademacher M, Zimmerman A W, et al. Spin-system heterogeneities indicate a selected-fit mechanism in fatty acid binding to heart-type fatty acid-binding protein(H-FABP)[J].Biochem J, 2001, 354:259-266. [28]石鹏飞,许家利,孙金魁,许厚强.关岭牛FABP1和FABP2基因克隆及其组织表达分析[J].南方农业学报, 2023, 54(2):598-608. [29]Masato F, Shigeyuki S, Kazuaki S, et al. Fatty acid binding protein 4(FABP4):Pathophysiological insightsand potent clinical biomarker of metabolic and cardiovascular diseases[J].Clin Med Insights Cardiol, 2014, 8(S3):23-33. [30]Ardicli S, Samli H, Alpay F, et al. Association of single nucleotide polymorphisms in the FABP4 gene with carcass characteristics and meat quality in Holstein bulls[J]. Ann Anim Sci, 2017, 17(1):117-130. [31]Niewold T A, Meinen M, Vand M J. Plasma intestinal fatty acid binding protein(I-FABP)concentrations increase following intestinal ischemia in pigs[J]. Res Vet Sci, 2004, 77(1):89-91. [32]王卓.延边牛FABP5、FABP6、DGAT1、USP43、P2RY10和FUBP3多态性与生长性状关联分析[D].延吉:延边大学,2023. [33]Michal J J, Zhang Z W, Gaskins C T, et al. The bovine fatty acid binding protein 4 gene is significantly associated with marbling and subcutaneous fat depth in Wagyu×Limousin F2crosses[J]. Anim Genet, 2006, 37(4):400-402. [34]Shin S C, Heo J P, Chung E R. Genetic variants of the FABP4gene are associated with marbling scores and meat quality grades in Hanwoo(Korean cattle)[J]. Mol Biol Rep, 2012,39(5):5323-5330. [35]Gerbens F, Verburg F J, Van Moerkerk H T, et al. Associations of heart and adipocyte fatty acid-binding protein gene expression with intramuscular fat content in pigs[J]. J Anim Sci,2001, 79(2):347-354. [36]廖秀冬,任立明,王光瑛,李昂,黄银花.北京鸭FABP2基因多态性与体尺和屠体性状的相关性研究[J].中国家禽,2012, 34(17):23-26. [37]徐松松,安荣荣,陈耀峰,程敏,李辉,王守志.鸡FABP2基因单倍型与生长和体组成性状的相关分析[J].中国家禽,2016, 38(8):5-9.
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doi: 10.19556/j.0258-7033.20241219-03
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出版时间:2025-12-16
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2种不同金属材料的力学参数
科 Family 属数 Number of genus 种数 Number of species 占总种数比例 Percentage of total species (%) 属 Genus 种数 Number of species 占总种数比例 Percentage of total species (%) 鹅膏菌科Amanitaceae 2 11 5.26 鹅膏菌属 Amanita 10 4.78 小菇科 Mycenaceae 2 12 5.74 丝盖伞属 Inocybe 5 2.39 多孔菌科 Polyporaceae 8 14 6.70 蜡蘑属 Laccaria 5 2.39 红菇科 Russulaceae 3 23 11.00 小皮伞属 Marasmius 6 2.87 小菇属 Mycena 11 5.26 光柄菇属 Pluteus 5 2.39 红菇属 Russula 17 8.13 栓菌属 Trametes 5 2.39
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