Aldehydic derivatives of bead cellulose?relationships between matrix structure and function in immobilization of enzymes catalyzing hydrolysis of high molecular substrates

1982 ◽  
Vol 24 (11) ◽  
pp. 2573-2582 ◽  
Author(s):  
P. Gemeiner ◽  
A. Breier
Keyword(s):  
Structure And Function ◽  
Matrix Structure ◽  
Immobilization Of Enzymes ◽  
Bead Cellulose ◽  
Molecular Substrates ◽  
And Function ◽  
Hydrolysis Of ◽  
Derivatives Of

scholarly journals Islands of complex DNA are widespread in Drosophila centric heterochromatin.

Genetics ◽  
1995 ◽  
Vol 141 (1) ◽  
pp. 283-303
Author(s):  
M H Le ◽  
D Duricka ◽  
G H Karpen
Keyword(s):  
Dna Sequences ◽  
Structure And Function ◽  
Southern Analysis ◽  
Cloning And Sequencing ◽  
Pulsed Field ◽  
Drosophila Heterochromatin ◽  
And Function ◽  
Heterochromatin Structure ◽  
Derivatives Of ◽  
Eukaryotic Genomes

Abstract Heterochromatin is a ubiquitous yet poorly understood component of multicellular eukaryotic genomes. Major gaps exist in our knowledge of the nature and overall organization of DNA sequences present in heterochromatin. We have investigated the molecular structure of the 1 Mb of centric heterochromatin in the Drosophila minichromosome Dp1187. A genetic screen of irradiated minichromosomes yielded rearranged derivatives of Dp1187 whose structures were determined by pulsed-field Southern analysis and PCR. Three Dp1187 deletion derivatives and an inversion had one breakpoint in the euchromatin and one in the heterochromatin, providing direct molecular access to previously inaccessible parts of the heterochromatin. End-probed pulsed-field restriction mapping revealed the presence of at least three "islands" of complex DNA, Tahiti, Moorea, and Bora Bora, constituting approximately one half of the Dp1187 heterochromatin. Pulsed-field Southern analysis demonstrated that Drosophila heterochromatin in general is composed of alternating blocks of complex DNA and simple satellite DNA. Cloning and sequencing of a small part of one island, Tahiti, demonstrated the presence of a retroposon. The implications of these findings to heterochromatin structure and function are discussed.

Morphological and Biochemical Features Affecting the Antithrombotic Properties of the Aorta in Adult Rabbits and Rabbit Pups

1998 ◽  
Vol 79 (05) ◽  
pp. 1034-1040 ◽  
Author(s):  
E. Nitschmann ◽  
L. Berry ◽  
S. Bridge ◽  
M. W. C. Hatton ◽  
M. Richardson ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Gel Electrophoresis ◽  
Arterial Wall ◽  
Structure And Function ◽  
Wall Structure ◽  
Matrix Structure ◽  
Antithrombotic Activity ◽  
Antithrombin Activity ◽  
And Function ◽  
Biochemical Features

SummaryWe hypothesised that there are important physiologic differences in arterial wall structure and function with respect to antithrombotic activity in the very young (pre-puberty) compared to adults. Electron microscopy, gel electrophoresis, and activity assays were used to examine differences in aorta structure and function comparing prepubertal rabbits (pups) to adult rabbits. Differences in endothelial function, extracellular matrix structure, proteoglycan (PG) distribution and glycosaminoglycan (GAG) content and function were shown. In both intima and media, total PG, chondroitin sulfate (CS) PG and heparan sulfate (HS) PG content were significantly increased in pups compared to adult rabbits. These findings corresponded to increased concentrations by mass analyses of CS GAG and DS GAG in aortas from pups. There was also a significant increase in antithrombin activity in pups due to HS GAG. In conclusion, differences in both structure and antithrombin activity of aortas from pups compared to adult rabbits suggest that young arteries may have greater antithrombotic potential that is, at least in part, related to increased HS GAG.

scholarly journals Breast cancer cell cyclooxygenase-2 expression alters extracellular matrix structure and function and numbers of cancer associated fibroblasts

Oncotarget ◽  
2017 ◽  
Vol 8 (11) ◽  
pp. 17981-17994 ◽  
Author(s):  
Balaji Krishnamachary ◽  
Ioannis Stasinopoulos ◽  
Samata Kakkad ◽  
Marie-France Penet ◽  
Desmond Jacob ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Extracellular Matrix ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Structure And Function ◽  
Cyclooxygenase 2 ◽  
Cancer Associated Fibroblasts ◽  
Matrix Structure ◽  
And Function

scholarly journals MT1-MMP–Dependent Remodeling of Cardiac Extracellular Matrix Structure and Function Following Myocardial Infarction

2012 ◽  
Vol 180 (5) ◽  
pp. 1863-1878 ◽  
Author(s):  
Gerald C. Koenig ◽  
R. Grant Rowe ◽  
Sharlene M. Day ◽  
Farideh Sabeh ◽  
Jeffrey J. Atkinson ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
Extracellular Matrix ◽  
Structure And Function ◽  
Matrix Structure ◽  
And Function

scholarly journals Structure and Function of Nucleoside Hydrolases from Physcomitrella patens and Maize Catalyzing the Hydrolysis of Purine, Pyrimidine, and Cytokinin Ribosides

2013 ◽  
Vol 163 (4) ◽  
pp. 1568-1583 ◽  
Author(s):  
M. Kopecna ◽  
H. Blaschke ◽  
D. Kopecny ◽  
A. Vigouroux ◽  
R. Koncitikova ◽  
...  
Keyword(s):  
Physcomitrella Patens ◽  
Structure And Function ◽  
Nucleoside Hydrolases ◽  
And Function ◽  
Hydrolysis Of ◽  
Purine Pyrimidine

TBC Proteins: Miraculous Regulators of Rabs GTPase Molecular Switches

2021 ◽  
Author(s):  
Jun Yan ◽  
Yingcheng Zheng ◽  
Song Han ◽  
Jun Yin ◽  
Yinping Li ◽  
...  
Keyword(s):  
Amino Acids ◽  
Intracellular Transport ◽  
Molecular Switches ◽  
Small Gtpases ◽  
Structure And Function ◽  
Rab Gtpase ◽  
Cellular Functions ◽  
Eukaryotic Proteins ◽  
And Function ◽  
Hydrolysis Of

TBC proteins are classified as a group because they contain a common conserved structure TBC domain. TBC domain consists of approximately 200 amino acids and presents in many eukaryotic proteins. It is reported that TBC proteins have been shown to function as a GAP for Rab GTPase. TBC proteins catalyze the hydrolysis of GTP and promote the conversion of Rab-GTP to Rab-GDP, thus participating in the specific intracellular transport. Many TBC proteins play important roles in cellular functions in mammals, and their deletions or mutations are closely related to many diseases. It is important to systematically sort out these findings and functions of the TBC family and illuminate the significance of TBC proteins in different physiological conditions. Here we reviewed the structure and function of TBC proteins, especially the function related to to Rab small GTPases.

scholarly journals The effects of tyrosine nitration on the structure and function of hen egg-white lysozyme

1996 ◽  
Vol 315 (2) ◽  
pp. 473-479 ◽  
Author(s):  
Paul G. RICHARDS ◽  
David J. WALTON ◽  
John HEPTINSTALL
Keyword(s):  
Cell Wall ◽  
Egg White ◽  
Structure And Function ◽  
Tyrosine Nitration ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
And Function ◽  
Hydrolysis Of ◽  
Hen Egg

We have investigated the effects of tyrosine nitration (to form the weak acid, 3-nitrotyrosine) at positions 23 or 20 plus 23, on the structure and function of hen egg-white lysozyme. Enzyme activity against Micrococcus luteus cell-wall fragments or soluble substrates exhibits two phenomena. (a) A decrease in Km and kcat for the hydrolysis of soluble oligo- and poly-saccharides, resulting in only minor changes in the catalytic efficiency (kcat/Km) upon nitration. (b) The hydrolysis of M. luteus cell-wall fragments appeared to be dominated by electrostatic interactions with the protein, giving a decrease in enzyme activity as the 3-nitrotyrosyl group became ionized. Removal of the cell-wall anionic polymer, teichuronic acid, from M. luteus abolished this effect. The 3-nitrotyrosine group was also found to act as a fluorescence quencher of exposed tryptophan residues in lysozyme.

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