Substrate-permeable encapsulation of enzymes maintains effective activity, stabilizes against denaturation, and protects against proteolytic degradation.
about
Protein encapsulation in liposomes: efficiency depends on interactions between protein and phospholipid bilayerMutation of exposed hydrophobic amino acids to arginine to increase protein stabilityImprovement of Drosophila acetylcholinesterase stability by elimination of a free cysteine.Allosteric inhibition of individual enzyme molecules trapped in lipid vesicles.The effect of engineered disulfide bonds on the stability of Drosophila melanogaster acetylcholinesterase.Amyloglucosidase enzymatic reactivity inside lipid vesicles.Encapsulation of enzymes in liposomes: high encapsulation efficiency and control of substrate permeability.Polymer micro- and nanocapsules as biological carriers with multifunctional properties.Template synthesis of test tube nanoparticles using non-destructive replicationAlbumin/asparaginase capsules prepared by ultrasound to retain ammonia.Electrochemical Biosensors - Sensor Principles and Architectures.Rate of solute incorporation to liposomes evaluated from encapsulated enzymes activities.Protein containers--promising tools for the future.Spontaneously formed semipermeable organic-inorganic hybrid vesicles permitting molecular weight selective transmembrane passage.Rapid and efficient method for the size separation of homogeneous fluorescein-encapsulating liposomes.Observing proteins as single molecules encapsulated in surface-tethered polymeric nanocontainers.Perforated bicontinuous cubic phases with pH-responsive topological channel interconnectivity.Microencapsulation of maltogenic α-amylase in poly(urethane-urea) shell: inverse emulsion method.Nanoengineered polymer capsules: tools for detection, controlled delivery, and site-specific manipulation.
P2860
Q24792568-AEE39196-26E0-45A7-B45B-1417FA09500FQ24792896-467A18E6-E733-4DF1-AF2C-047BDA92793AQ24798604-EA4319C8-7AF6-4D99-AAF2-AC4D098B7DC3Q30514333-F5FBEBE7-FEC5-468A-9925-008DC32F6392Q33242982-9B758ECA-6357-4A8A-AF92-B01D6A05A7D9Q33319648-7A4D7F23-012B-4E5E-992A-DC6617F12223Q34306621-821A2487-2704-488C-A7C5-7229E99A577CQ35116954-A7D5C439-5055-4B3D-9716-43900D0B39E0Q36946769-4F0CD542-C65E-4F2C-AB46-F1A4B02CEB57Q38740125-17BE77C1-6000-4DFB-A321-800AC0AFF7A4Q39018116-E25BF00A-5848-4D4A-9961-0571F53AB540Q39310113-2CB97F2B-0D72-43E3-982D-54BFE8C43B0EQ39743921-0B8F5985-0A22-4390-8687-64DD6372B2B6Q44290609-83CF0C15-805C-4FE8-A971-BE0C0EA8930DQ45974649-05E6FDC4-E0EA-482A-AD9D-F80EADA889DEQ46134643-DA21DB19-73EE-47E6-80BB-DB5CF9B7FD4FQ46141995-7D145DF8-6504-4084-8DC1-FBC8AF5D5DC6Q47673979-538F8ABF-FC55-4742-947E-AFD99DFF1E56Q51090626-86DC93F9-D966-4549-855B-8D61A34DCAA7
P2860
Substrate-permeable encapsulation of enzymes maintains effective activity, stabilizes against denaturation, and protects against proteolytic degradation.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh-hant
name
Substrate-permeable encapsulat ...... ainst proteolytic degradation.
@en
Substrate-permeable encapsulat ...... ainst proteolytic degradation.
@nl
type
label
Substrate-permeable encapsulat ...... ainst proteolytic degradation.
@en
Substrate-permeable encapsulat ...... ainst proteolytic degradation.
@nl
prefLabel
Substrate-permeable encapsulat ...... ainst proteolytic degradation.
@en
Substrate-permeable encapsulat ...... ainst proteolytic degradation.
@nl
P2093
P2860
P356
P1476
Substrate-permeable encapsulat ...... ainst proteolytic degradation.
@en
P2093
P2860
P304
P356
10.1002/BIT.10074
P577
2001-12-01T00:00:00Z