DISTRIBUTION OF HEXOSAMINE IN ELEGTROPHORETIC FRACTIONS OF AVIAN, BOVINE, PORCINE, AND HUMAN SERA

1967 ◽  
Vol 45 (4) ◽  
pp. 541-550 ◽  
Author(s):  
A. P. Gaunce ◽  
P. A. Anastassiadis
Keyword(s):  
Human Blood ◽  
Filter Paper ◽  
Cationic Resin ◽  
Human Sera ◽  
Hydrolysis Of ◽  
Direct Hydrolysis

The distribution of hexosamine among the proteins of avian, bovine, porcine, and human blood sera was studied by electrophoresis on filter paper. Hexosamine was determined after direct hydrolysis of stained sections of the paper, followed by chromatography of hydrolysates on cationic resin. Some substantial and statistically significant differences in hexosamine and protein contents of the zones were found among species.

scholarly journals Improvement of Enzymatic Saccharification of Cellulose-Containing Raw Materials Using Aspergillus niger

Processes ◽  
2021 ◽  
Vol 9 (8) ◽  
pp. 1360
Author(s):  
Ekaterina Budenkova ◽  
Stanislav Sukhikh ◽  
Svetlana Ivanova ◽  
Olga Babich ◽  
Vyacheslav Dolganyuk ◽  
...  
Keyword(s):  
Enzymatic Hydrolysis ◽  
Aspergillus Niger ◽  
Filter Paper ◽  
Raw Materials ◽  
Enzymatic Saccharification ◽  
Wood Chip ◽  
Cellulase Activity ◽  
Wood Chips ◽  
Acid Pretreatment ◽  
Hydrolysis Of

Enzymatic hydrolysis of cellulose-containing raw materials, using Aspergillus niger, were studied. Filter paper, secondary cellulose-containing or starch-containing raw materials, miscanthus cellulose after alkaline or acid pretreatment, and wood chip cellulose, were used as substrates. The study focused on a wild A. niger strain, treated, or not (control), by ultraviolet (UV) irradiations for 45, 60, or 120 min (UV45, UV60, or UV120), or by UV irradiation for 120 min followed by a chemical treatment with NaN3 + ItBr for 30 min or 80 min (UV120 + CH30 or UV120 + CH80). A mixture of all the A. niger strains (MIX) was also tested. A citrate buffer, at 50 mM, wasthe most suitable for enzymatic hydrolysis. As the UV exposure time increased to 2 h, the cellulase activity of the surviving culturewas increased (r = 0.706; p < 0.05). The enzymatic activities of the obtained strains, towards miscanthus cellulose, wood chips, and filter paper, were inferior to those obtained with commercial enzymes (8.6 versus 9.1 IU), in some cases. Under stationary hydrolysis at 37 °C, pH = 4.7, the enzymatic activity of A. niger UV120 + CH30 was 24.9 IU. The enzymatic hydrolysis of secondary raw materials, using treated A. niger strains, was themost effective at 37 °C. Similarly, the most effective treatment of miscanthus cellulose and wood chips occurred at 50 °C. The maximum conversion of cellulose to glucose was observed using miscanthus cellulose (with alkaline pretreatment), and the minimum conversion was observed when using wood chips. The greatest value of cellulase activity was evidenced in the starch-containing raw materials, indicating that A. niger can ferment not only through cellulase activity, but also via an amylolytic one.

Two neutral thermostable cellulases from Phialophora sp. G5 act synergistically in the hydrolysis of filter paper

2012 ◽  
Vol 121 ◽  
pp. 404-410 ◽  
Author(s):  
Junqi Zhao ◽  
Pengjun Shi ◽  
Zhongyuan Li ◽  
Peilong Yang ◽  
Huiying Luo ◽  
...  
Keyword(s):  
Filter Paper ◽  
Hydrolysis Of

Discordant results for determinations of triglycerides in pig sera

1993 ◽  
Vol 39 (1) ◽  
pp. 125-128 ◽  
Author(s):  
T Tuten ◽  
K A Robinson ◽  
D S Sgoutas
Keyword(s):  
Gas Liquid Chromatography ◽  
Glycerol Phosphate ◽  
Serum Triglycerides ◽  
Lipolytic Enzymes ◽  
Chemical Hydrolysis ◽  
Human Sera ◽  
Microbial Lipases ◽  
Sample Method ◽  
Hydrolysis Of ◽  
Enzymatic Methods

Abstract We recently determined triglyceride concentrations in pig sera by three fully enzymatic methods (Kodak Ektachem 700, Hitachi 707, and Abbott EPx) and obtained significantly lower values than those obtained with chemical or enzymatic methods based on chemical hydrolysis. All methods used involve microbial lipases for liberating glycerol from glycerides and glycerol phosphate dehydrogenases or oxidases for subsequent oxidation. The methods were validated against reference methods by using fresh human sera and survey materials. The discordant results were not from matrix sample-method interaction but from incomplete hydrolysis of pig serum triglycerides by the lipolytic enzymes. When serum triglycerides from 10 pigs showing the highest biases were hydrolyzed by microbial lipases and the reaction mixture was subjected to thin-layer and gas-liquid chromatography, the predominant end products were palmitoyl monoglyceride and a mixture of free fatty acids with the following composition (fatty acid as percent of total +/- SD): 16:0, 7.8 +/- 2; 18:0, 5.4 +/- 2.2; 18:1, 53 +/- 12; 18:2, 31 +/- 4.6; and 18:3, 2.5 +/- 1. Assuming that the lipases exhibit the usual specificity toward the 1 and 3 positions of the triglyceride, the data suggest that, in pig, triglycerides 18:1 and 18:2 occupy the 1 and 3 positions and 16:0 (palmitic acid) predominantly occupies the 2 position. Triglycerides of this structure may not be well hydrolyzed by the typical lipolytic enzymes in clinical assays.

Detection of cellulase inhibitor in the wheat bran culture of Aspergillus terreus

1981 ◽  
Vol 27 (12) ◽  
pp. 1334-1340 ◽  
Author(s):  
S. N. Sinha ◽  
B. L. Ghosh ◽  
S. N. Ghose
Keyword(s):  
Molecular Weight ◽  
Wheat Bran ◽  
Filter Paper ◽  
Aspergillus Terreus ◽  
Defined Medium ◽  
Low Molecular Weight ◽  
Chemically Defined Medium ◽  
Plant Origin ◽  
First Time ◽  
Hydrolysis Of

The presence of a cellulase inhibitor in the wheat bran culture of a fungus is reported for the first time. The inhibitor has a low molecular weight and is relatively stable to heat. It is absent from wheat bran and is not produced in a chemically defined medium. Unlike cellulase inhibitors of plant origin, this inhibitor is not a polyphenol. It inhibits the hydrolysis of cotton to a greater degree than that of filter paper or carboxymethylcellulose. In addition to inhibiting Aspergillus terreus cellulase, it also inhibits a variety of commercial cellulases.

scholarly journals Rapid formation of inositol 1,3,4,5-tetrakisphosphate and inositol 1,3,4-trisphosphate in rat parotid glands may both result indirectly from receptor-stimulated release of inositol 1,4,5-trisphosphate from phosphatidylinositol 4,5-bisphosphate

1986 ◽  
Vol 238 (2) ◽  
pp. 507-516 ◽  
Author(s):  
P T Hawkins ◽  
L Stephens ◽  
C P Downes
Keyword(s):  
Initial Rate ◽  
Parotid Glands ◽  
Inositol 1,4,5 Trisphosphate ◽  
Rapid Formation ◽  
Inositol Tetrakisphosphate ◽  
Rat Parotid ◽  
Phosphatidylinositol 4 ◽  
Hydrolysis Of ◽  
Direct Hydrolysis ◽  
Stimulation Of

Addition of 1 mM-carbachol to [3H]inositol-labelled rat parotid slices stimulated rapid formation of [3H]inositol 1,3,4,5-tetrakisphosphate, the accumulation of which reached a peak 20 s after stimulation, and then declined rapidly towards a new steady state. The initial rate of formation of inositol 1,3,4,5-tetrakisphosphate was slower than that for inositol 1,4,5-trisphosphate. The radioactivity in [3H]inositol 1,3,4,5-tetrakisphosphate fell quickly in carbachol-stimulated and then atropine-blocked parotid slices, suggesting that it is rapidly metabolized during stimulation. Parotid homogenates rapidly dephosphorylated inositol 1,4,5-trisphosphate, inositol 1,3,4,5-tetrakisphosphate and, less rapidly, inositol 1,3,4-trisphosphate. Inositol 1,3,4,5-tetrakisphosphate was specifically hydrolysed to a compound with the chromatographic properties of inositol 1,3,4-trisphosphate. The only 3H-labelled phospholipids that we could detect in parotid slices labelled with [3H]inositol for 90 min were phosphatidylinositol, phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-bisphosphate. Parotid homogenates synthesized inositol tetrakisphosphate from inositol 1,4,5-trisphosphate. This activity was dependent on the presence of ATP. We suggest that, during carbachol stimulation of parotid slices, the key event in inositol lipid metabolism is the activation of phosphatidylinositol 4,5-bisphosphate-specific phospholipase C. The inositol 1,4,5-trisphosphate thus liberated is metabolized in two distinct ways; by direct hydrolysis of the 5-phosphate to form inositol 1,4-bisphosphate and by phosphorylation to form inositol 1,3,4,5-tetrakisphosphate and hence, by hydrolysis of this tetrakisphosphate, to form inositol 1,3,4-trisphosphate.

scholarly journals ON INDIVIDUAL DIFFERENCES IN HUMAN BLOOD

1928 ◽  
Vol 47 (5) ◽  
pp. 757-775 ◽  
Author(s):  
K. Landsteiner ◽  
Philip Levine
Keyword(s):  
Individual Differences ◽  
Human Blood ◽  
Blood Groups ◽  
The Body ◽  
Serological Evidence ◽  
Clear Cut ◽  
Human Sera ◽  
Normal Human ◽  
High Degree ◽  
Biochemical Differentiation

A clear-cut differentiation of human blood, aside from the blood groups, could be made by means of special agglutinating immune sera. The observations point to the existence of several agglutinable factors for which no agglutinins are demonstrable in normal human sera. In view of the latter circumstance the results reported do not imply any change in the scheme of the four blood groups. The body of serological evidence leads to the inference of a high degree of biochemical differentiation among individuals.

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