Elucidation of the chemical nature of the steady-state intermediates in the mechanism of carboxypeptidase A

Biochemistry ◽  
1986 ◽  
Vol 25 (3) ◽  
pp. 646-651 ◽  
Author(s):  
A. Galdes ◽  
D. S. Auld ◽  
B. L. Vallee
Keyword(s):  
Steady State ◽  
Chemical Nature ◽  
Carboxypeptidase A

scholarly journals Structure and Dynamics of the Metal Site of Cadmium-Substituted Carboxypeptidase A in Solution and Crystalline States and under Steady-State Peptide Hydrolysis†

Biochemistry ◽  
1997 ◽  
Vol 36 (38) ◽  
pp. 11514-11524 ◽  
Author(s):  
Rogert Bauer ◽  
Eva Danielsen ◽  
Lars Hemmingsen ◽  
Marianne V. Sørensen ◽  
Jens Ulstrup ◽  
...  
Keyword(s):  
Steady State ◽  
Carboxypeptidase A ◽  
Peptide Hydrolysis ◽  
Metal Site ◽  
Structure And Dynamics

scholarly journals The steady-state kinetics of peroxidase with 2,2′-azino-di-(3-ethyl-benzthiazoline-6-sulphonic acid) as chromogen

1975 ◽  
Vol 145 (1) ◽  
pp. 93-103 ◽  
Author(s):  
R E Childs ◽  
W G Bardsley
Keyword(s):  
Steady State ◽  
Kinetic Analysis ◽  
Chemical Nature ◽  
Spectroscopic Properties ◽  
Sulphonic Acid ◽  
Steady State Kinetics ◽  
Novel Methods ◽  
Kinetics Of ◽  
Substrate Concentrations

The chemical nature of the important new chromogen ABTS [2,2'-azino-di-(3-ethyl-benzthiazoline-6-sulphonic acid)] is described together with an account of the redox and spectroscopic properties of the system ABTS--H2O2--peroxidase. Keq. is calculated and a study of the steady-state kinetics over a whole range of substrate concentrations is reported. By using novel methods of kinetic analysis, an interpretation of the results is given which requires some extension of the classical peroxidase mechanism.

Studies on Water in the Hydration Chamber of a Modified Electron Microscope

1970 ◽  
Vol 28 ◽  
pp. 544-545
Author(s):  
R. C. Moretz ◽  
G. G. Hausner ◽  
D. F. Parsons
Keyword(s):  
Thin Film ◽  
Thin Films ◽  
Electron Microscope ◽  
Steady State ◽  
Room Temperature ◽  
Small Mass ◽  
Equilibrium Pressure ◽  
Biological Objects ◽  
Mechanical Pump ◽  
Differential Pumping

Use of the electron microscope to examine wet objects is possible due to the small mass thickness of the equilibrium pressure of water vapor at room temperature. Previous attempts to examine hydrated biological objects and water itself used a chamber consisting of two small apertures sealed by two thin films. Extensive work in our laboratory showed that such films have an 80% failure rate when wet. Using the principle of differential pumping of the microscope column, we can use open apertures in place of thin film windows.Fig. 1 shows the modified Siemens la specimen chamber with the connections to the water supply and the auxiliary pumping station. A mechanical pump is connected to the vapor supply via a 100μ aperture to maintain steady-state conditions.

Release of Neurosecretion in the Crayfish Sinus Gland

1968 ◽  
Vol 26 ◽  
pp. 150-151
Author(s):  
Richard R. Shivers
Keyword(s):  
Chemical Nature ◽  
Storage Site ◽  
Neurosecretory Granules ◽  
Sinus Gland ◽  
Diameter Class ◽  
Dense Membrane ◽  
Neurohemal Organ ◽  
Dense Vesicles

The sinus gland is a neurohemal organ located in the crayfish eyestalk and represents a storage site for neurohormones prior to their release into the circulation. The sinus gland contains 3 classes of dense, membrane-limited granules: 1) granules measuring less than 1000 Å in diameter, 2) granules measuring 1100-1400 Å in diameter, and 3) granules measuring 1500-2000 Å in diameter. Class 3 granules are the most electron-dense of the granules found in the sinus gland, while class 2 granules are the most abundant. Generally, all granules appear to undergo similar changes during release.Release of neurosecretory granules may be initiated by a preliminary fragmentation of the “parent granule” into smaller, less dense vesicles which measure about 350 Å in diameter (V, Figs. 1-3). A decrease in density of the granules prior to their fragmentation has been observed and may reflect a change in the chemical nature of the granule contents.

The protease phenotype and crystalline nature of the granules of intraepithelial mast cells in Trichinella spiralis-infected mice

1995 ◽  
Vol 53 ◽  
pp. 818-819
Author(s):  
D.S. Friend ◽  
N. Ghildyal ◽  
M.F. Gurish ◽  
K.F. Austen ◽  
R.L. Stevens
Keyword(s):  
Small Intestine ◽  
Mast Cells ◽  
Epithelial Cells ◽  
Lamina Propria ◽  
Trichinella Spiralis ◽  
Intestinal Epithelial ◽  
Carboxypeptidase A ◽  
C3h Mice ◽  
Granule Morphology ◽  
Crystalline Nature

Trichinella spiralis induces a profound mastocytosis and eosinophilia in the small intestine of the infected mouse. Mouse mast cells (MC) store in their granules various combinations of at least five chymotryptic chymases [designated mouse MC protease (mMCP) 1 to 5], two tryptic proteases designated mMCP-6 and mMCP-7 and an exopeptidase, carboxypeptidase A (mMC-CPA). Using antipeptide, protease -specific antibodies to these MC granule proteases, immunohistochemistry was done to determine the distribution, number and protease phenotype of the MCs in the small intestine and spleen 10 to >60 days after Trichinella infection of BALB/c and C3H mice. TEM was performed to evaluate the granule morphology of the MCs between intestinal epithelial cells and in the lamina propria (mucosal MCs) and in the submucosa, muscle and serosa of the intestine (submucosal MCs).As noted in the table below, the number of submucosal MCs remained constant throughout the study. In contrast, on day 14, the number of MCs in the mucosa increased ~25 fold. Increased numbers of MCs were observed between epithelial cells in the mucosal crypts, in the lamina propria and to a lesser extent, between epithelial cells of the intestinal villi.

Freeze-fracture cytochemistry: A goal set by Russell Steere in 1957

1993 ◽  
Vol 51 ◽  
pp. 60-61
Author(s):  
Nicholas J Severs
Keyword(s):  
Chemical Nature ◽  
Biological Systems ◽  
Freeze Fracture ◽  
Structural Components ◽  
Major Goal ◽  
Membrane Biology ◽  
Routine Application ◽  
The Future ◽  
Freeze Etching

In his pioneering demonstration of the potential of freeze-etching in biological systems, Russell Steere assessed the future promise and limitations of the technique with remarkable foresight. Item 2 in his list of inherent difficulties as they then stood stated “The chemical nature of the objects seen in the replica cannot be determined”. This defined a major goal for practitioners of freeze-fracture which, for more than a decade, seemed unattainable. It was not until the introduction of the label-fracture-etch technique in the early 1970s that the mould was broken, and not until the following decade that the full scope of modern freeze-fracture cytochemistry took shape. The culmination of these developments in the 1990s now equips the researcher with a set of effective techniques for routine application in cell and membrane biology.Freeze-fracture cytochemical techniques are all designed to provide information on the chemical nature of structural components revealed by freeze-fracture, but differ in how this is achieved, in precisely what type of information is obtained, and in which types of specimen can be studied.

Continuous hydrogenolysis of acetal-stabilized lignin in flow

2021 ◽  
Author(s):  
Wu Lan ◽  
Yuan Peng Du ◽  
Songlan Sun ◽  
Jean Behaghel de Bueren ◽  
Florent Héroguel ◽  
...  
Keyword(s):  
Steady State ◽  
Challenges And Opportunities

We performed a steady state high-yielding depolymerization of soluble acetal-stabilized lignin in flow, which offered a window into challenges and opportunities that will be faced when continuously processing this feedstock.

Network reconstruction based on steady-state data

2008 ◽  
Vol 45 ◽  
pp. 161-176 ◽  
Author(s):  
Eduardo D. Sontag
Keyword(s):  
Steady State ◽  
Reverse Engineering ◽  
Theoretical Method ◽  
Network Reconstruction ◽  
Quasi Steady State ◽  
State Data

This paper discusses a theoretical method for the “reverse engineering” of networks based solely on steady-state (and quasi-steady-state) data.

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