scholarly journals Role of Pregastric Esterase in the Abomasal Hydrolysis of Milk Fat in the Young Calf

1961 ◽  
Vol 44 (12) ◽  
pp. 2227-2231 ◽  
Author(s):  
H.A. Ramsey ◽  
J.W. Young
Keyword(s):  
Milk Fat ◽  
Molecules ◽  
2021 ◽  
Vol 26 (10) ◽  
pp. 2852
Author(s):  
Paul A. Foster

Steroid sulphatase (STS), involved in the hydrolysis of steroid sulphates, plays an important role in the formation of both active oestrogens and androgens. Since these steroids significantly impact the proliferation of both oestrogen- and androgen-dependent cancers, many research groups over the past 30 years have designed and developed STS inhibitors. One of the main contributors to this field has been Prof. Barry Potter, previously at the University of Bath and now at the University of Oxford. Upon Prof. Potter’s imminent retirement, this review takes a look back at the work on STS inhibitors and their contribution to our understanding of sulphate biology and as potential therapeutic agents in hormone-dependent disease. A number of potent STS inhibitors have now been developed, one of which, Irosustat (STX64, 667Coumate, BN83495), remains the only one to have completed phase I/II clinical trials against numerous indications (breast, prostate, endometrial). These studies have provided new insights into the origins of androgens and oestrogens in women and men. In addition to the therapeutic role of STS inhibition in breast and prostate cancer, there is now good evidence to suggest they may also provide benefits in patients with colorectal and ovarian cancer, and in treating endometriosis. To explore the potential of STS inhibitors further, a number of second- and third-generation inhibitors have been developed, together with single molecules that possess aromatase–STS inhibitory properties. The further development of potent STS inhibitors will allow their potential therapeutic value to be explored in a variety of hormone-dependent cancers and possibly other non-oncological conditions.


1983 ◽  
Vol 258 (22) ◽  
pp. 13673-13679 ◽  
Author(s):  
A Gómez-Puyou ◽  
G Ayala ◽  
U Muller ◽  
M Tuena de Gómez-Puyou

2016 ◽  
Vol 199 ◽  
pp. 49-58 ◽  
Author(s):  
Shaoni Sun ◽  
Shaolong Sun ◽  
Xuefei Cao ◽  
Runcang Sun

2015 ◽  
Vol 1 (7) ◽  
pp. e1500263 ◽  
Author(s):  
Akihiko Nakamura ◽  
Takuya Ishida ◽  
Katsuhiro Kusaka ◽  
Taro Yamada ◽  
Shinya Fushinobu ◽  
...  

Hydrolysis of carbohydrates is a major bioreaction in nature, catalyzed by glycoside hydrolases (GHs). We used neutron diffraction and high-resolution x-ray diffraction analyses to investigate the hydrogen bond network in inverting cellulase PcCel45A, which is an endoglucanase belonging to subfamily C of GH family 45, isolated from the basidiomycete Phanerochaete chrysosporium. Examination of the enzyme and enzyme-ligand structures indicates a key role of multiple tautomerizations of asparagine residues and peptide bonds, which are finally connected to the other catalytic residue via typical side-chain hydrogen bonds, in forming the “Newton’s cradle”–like proton relay pathway of the catalytic cycle. Amide–imidic acid tautomerization of asparagine has not been taken into account in recent molecular dynamics simulations of not only cellulases but also general enzyme catalysis, and it may be necessary to reconsider our interpretation of many enzymatic reactions.


1991 ◽  
Vol 56 (1) ◽  
pp. 234-237 ◽  
Author(s):  
JYH-PING CHEN ◽  
HONG PAI

1988 ◽  
Vol 255 (3) ◽  
pp. 895-899 ◽  
Author(s):  
J Woodward ◽  
M Lima ◽  
N E Lee

Microcrystalline cellulose (10 mg of Avicel/ml) was hydrolysed to glucose by different concentrations of the purified cellulase components endoglucanase (EG) II and cellobiohydrolases (CBH) I and II, alone and in combination with each other, in the presence of excess beta-glucosidase. At a concentration of 360 micrograms/ml (160 micrograms of EG II/ml, 100 micrograms of CBH I/ml and 100 micrograms of CBH II/ml) the degree of synergism among them was negligible. As the concentration of cellulase decreased, the degree of synergism increased, reaching an optimum at 20 micrograms/ml (5 micrograms of EG II/ml, 10 micrograms of CBH I/ml and 5 micrograms of CBH II/ml). There was no apparent relationship between the ratio of the components and the degree of synergism. The latter is probably due, though it could not be proved, to the level of saturation of the substrate with each component. Inhibition of Avicel hydrolysis was observed when the substrate was incubated with saturating and nonsaturating concentrations of a mixture of EG II and CBH I respectively. A similar result was also observed with a combination of EG I and EG II.


2007 ◽  
Vol 79 (4) ◽  
pp. 481-490 ◽  
Author(s):  
Angelo Fontana ◽  
Giuliana d'Ippolito ◽  
Adele Cutignano ◽  
Antonio Miralto ◽  
Adrianna Ianora ◽  
...  

Oxylipins are important signal transduction molecules widely distributed in animals and plants where they regulate a variety of events associated with physiological and pathological processes. The family embraces several different metabolites that share a common origin from the oxygenase-catalyzed oxidation of polyunsaturated fatty acids. The biological role of these compounds has been especially studied in mammalians and higher plants, although a varied and very high concentration of these products has also been reported from marine macroalgae. This article gives a summary of our results concerning the oxylipin chemistry of marine diatoms, a major class of planktonic microalgae that discourage predation from their natural grazers, zooplanktonic copepods, using chemical warfare. These apparently harmless microscopic cells produce a plethora of oxylipins, including short-chain unsaturated aldehydes, hydroxyl-, keto-, and epoxyhydroxy fatty acid derivatives, that induce reproductive failure in copepods through abortions, congenital malformations, and reduced larval growth. The biochemical process involved in the production of these compounds shows a simple regulation based on decompartmentation and mixing of preexisting enzymes and requires hydrolysis of chloroplast-derived glycolipids to feed the downstream activities of C16 and C20 lipoxygenases.


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