T6763
Trypsin Acetylated from bovine pancreas
Type V-S, ≥8,500 BAEE units/mg protein (biuret)
Sinónimos:
Acetyltrypsin
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Specific activity:
≥8,500 BAEE units/mg protein (biuret)
Biological source:
bovine pancreas
Servicio técnico
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Permítanos ayudarlebiological source
bovine pancreas
Quality Level
type
Type V-S
form
powder
specific activity
≥8,500 BAEE units/mg protein (biuret)
UniProt accession no.
storage temp.
−20°C
Gene Information
cow ... TRYP8(282603)
General description
The trypsin molecule has two domains: one is related to the enzyme active site and the tryptophan residues; the other is related to the 8-anilinonaphthalene-1-sulfonate binding.
Application
Trypsin has been used in a study to assess the ontogeny of the endocrine pancreas in the fetal/newborn baboon. Trypsin digestion and hydrogen/deuterium exchange support the transition between inward- and outward-facing conformations during the catalytic cycle of the bacterial multidrug ATP-binding cassette transporter.
Biochem/physiol Actions
Lys-acetylated trypsin is less susceptible to autolysis than the native form.
Preparation Note
Prepared by the method of Labouesse, J. and Gervais, M., Eur. J. Biochem., 2, 215 (1967).
Other Notes
One BAEE unit will produce a ΔA253 of 0.001 per min at pH 7.6 at 25° C using BAEE as substrate. Reaction volume = 3.2 mL (1 cm light path).
View more information on trypsin at www.sigma-aldrich.com/enzymeexplorer.
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Clase de almacenamiento
11 - Combustible Solids
wgk
WGK 3
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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The Journal of endocrinology, 214(3), 289-299 (2012-06-23)
Erratic regulation of glucose metabolism including hyperglycemia is a common condition in premature infants and is associated with increased morbidity and mortality. The objective of this study was to examine histological and ultrastructural differences in the endocrine pancreas in fetal
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Shahid Mehmood et al.
Proceedings of the National Academy of Sciences of the United States of America, 109(27), 10832-10836 (2012-06-20)
The study of membrane proteins remains a challenging task, and approaches to unravel their dynamics are scarce. Here, we applied hydrogen/deuterium exchange (HDX) coupled to mass spectrometry to probe the motions of a bacterial multidrug ATP-binding cassette (ABC) transporter, BmrA