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Cocoonase. I. Preliminary characterization of a proteolytic enzyme from silk moths.

作者信息

Kafatos F C, Tartakoff A M, Law J H

出版信息

J Biol Chem. 1967 Apr 10;242(7):1477-87.

PMID:6023217
Abstract
摘要

相似文献

1
Cocoonase. I. Preliminary characterization of a proteolytic enzyme from silk moths.茧酶。一、家蚕蛋白水解酶的初步特性分析。
J Biol Chem. 1967 Apr 10;242(7):1477-87.
2
Functional expression of a Bombyx mori cocoonase: potential application for silk degumming.家蚕茧酶的功能表达:在丝胶脱胶中的潜在应用。
Acta Biochim Biophys Sin (Shanghai). 2012 Dec;44(12):974-83. doi: 10.1093/abbs/gms090.
3
Cocoonase. 3. Purification, preliminary characterization, and activation of the zymogen of an insect protease.
J Biol Chem. 1971 Jul 10;246(13):4131-7.
4
Properties of the Antheraea mylitta cocoonase.柞蚕茧酶的性质
Comp Biochem Physiol B. 1973 Feb 15;44(2):595-609. doi: 10.1016/0305-0491(73)90033-3.
5
An active recombinant cocoonase from the silkworm Bombyx mori: bleaching, degumming and sericin degrading activities.一种来自家蚕的活性重组茧酶:漂白、脱胶和丝胶降解活性。
J Sci Food Agric. 2015 Apr;95(6):1179-89. doi: 10.1002/jsfa.6806. Epub 2014 Aug 4.
6
The cocoonase zymogen cells of silk moths: a model of terminal cell differentiation for specific protein synthesis.蚕蛾的茧酶原细胞:特定蛋白质合成的终末细胞分化模型。
Curr Top Dev Biol. 1972;7:125-91. doi: 10.1016/s0070-2153(08)60071-x.
7
Purification and characterization of cocoonase from the silkworm Bombyx mori.家蚕茧酶的纯化与特性分析
Biosci Biotechnol Biochem. 2014;78(2):202-11. doi: 10.1080/09168451.2014.878215. Epub 2014 Apr 16.
8
Cocoonase. IV. Mechanism of activation of prococoonase from Antheraea polyphemus.
J Biol Chem. 1973 May 10;248(9):3012-20.
9
Activation of skeletal muscle phosphorylase kinase by Ca2+. II. Identification of the kinase activating factor as a proteolytic enzyme.钙离子对骨骼肌磷酸化酶激酶的激活作用。II. 激酶激活因子为蛋白水解酶的鉴定
Biochemistry. 1968 Jun;7(6):2116-22. doi: 10.1021/bi00846a014.
10
Alkaline proteases in digestive juice of the silkworm, Bombyx mori.家蚕消化液中的碱性蛋白酶。
Biochim Biophys Acta. 1982 Apr 21;703(1):1-10. doi: 10.1016/0167-4838(82)90002-4.

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1
Impression of Insect's Proteolytic Enzyme Cocoonase and Its Application: A Comprehensive Review.昆虫蛋白水解酶茧酶的研究进展及其应用:综述
Protein J. 2025 Feb;44(1):48-61. doi: 10.1007/s10930-024-10246-5. Epub 2025 Feb 4.
2
Identification of cocoonase and cocoonase like protein using polyclonal antibody of Antheraea mylitta cocoonase.利用蓖麻蚕茧酶多克隆抗体鉴定茧酶和茧酶样蛋白。
Biotechnol Lett. 2024 Feb;46(1):47-54. doi: 10.1007/s10529-023-03447-y. Epub 2023 Dec 18.
3
In silico structural and functional characterization of Antheraea mylitta cocoonase.
蓖麻蚕茧酶的计算机模拟结构与功能表征
J Genet Eng Biotechnol. 2022 Jul 11;20(1):102. doi: 10.1186/s43141-022-00367-8.
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Dynamic monitoring of vital functions and tissue re-organization in Saturnia pavonia (Lepidoptera, Saturniidae) during final metamorphosis by non-invasive MRI.非侵入性 MRI 技术对金星绢蝶(鳞翅目,大蚕蛾科)终末变态过程中生命功能和组织重组的动态监测。
Sci Rep. 2022 Jan 20;12(1):1105. doi: 10.1038/s41598-022-05092-3.
5
Pollen feeding in butterflies: the singular evolution of an adaptive suite.蝴蝶吸食花粉:一套适应性特征的独特演化
Proc Biol Sci. 2020 Nov 11;287(1938):20201304. doi: 10.1098/rspb.2020.1304.
6
Cocoonase is indispensable for Lepidoptera insects breaking the sealed cocoon.茧氨酸酶对于鳞翅目昆虫破茧而出是不可或缺的。
PLoS Genet. 2020 Sep 28;16(9):e1009004. doi: 10.1371/journal.pgen.1009004. eCollection 2020 Sep.
7
Evolutionary and structural analyses uncover a role for solvent interactions in the diversification of cocoonases in butterflies.进化和结构分析揭示了溶剂相互作用在蝴蝶茧酶多样化中的作用。
Proc Biol Sci. 2018 Jan 10;285(1870). doi: 10.1098/rspb.2017.2037.
8
Gene Duplication and Gene Expression Changes Play a Role in the Evolution of Candidate Pollen Feeding Genes in Heliconius Butterflies.基因复制和基因表达变化在红带袖蝶候选花粉取食基因的进化中发挥作用。
Genome Biol Evol. 2016 Sep 2;8(8):2581-96. doi: 10.1093/gbe/evw180.
9
"Disaggregation" of phytochrome in vitro-a consequence of proteolysis.植物色素在体外的“解聚”——蛋白水解的结果
Plant Physiol. 1971 Dec;48(6):686-93. doi: 10.1104/pp.48.6.686.
10
The packaging of a secretory protein. Kinetics of cocoonase zymogen transport into a storage vacuole.分泌蛋白的包装。茧酶原转运至储存液泡的动力学。
J Cell Biol. 1971 Feb;48(2):426-31. doi: 10.1083/jcb.48.2.426.