scholarly journals Purification and characterization of three distinct types of phospholipase A2 inhibitors from the blood plasma of the Chinese mamushi, Agkistrodon blomhoffii siniticus

1997 ◽  
Vol 325 (2) ◽  
pp. 527-531 ◽  
Author(s):  
Naoki OHKURA ◽  
Hiroaki OKUHARA ◽  
Seiji INOUE ◽  
Kiyoshi IKEDA ◽  
Kyozo HAYASHI
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Phospholipase A2 ◽  
Blood Plasma ◽  
Amino Acid Residues ◽  
Group Iii ◽  
Group I ◽  
Binding Surface ◽  
Group Ii

Three distinct types of phospholipase A2 (PLA2) inhibitory proteins (PLIα, PLIβ, and PLIγ) were isolated from the blood plasma of the Chinese mamushi, Agkistrodonblomhoffiisiniticus. PLIα is an inhibitor that we have already purified and whose amino acid sequence we have already determined [Ohkura, Inoue, Ikeda and Hayashi (1993) J. Biochem. (Tokyo) 113, 413–419]. It inhibited selectively the group-II acidic PLA2s from Crotalidae venom. PLIβ was a 160-kDa glycoprotein having a trimeric structure composed of 50-kDa subunits. The amino acid sequence of the first 30 amino acids of the N-terminal part of the 50-kDa subunit was determined and found to have no significant homology to that of known proteins. PLIβ was a selective inhibitor against the group-II basic PLA2s from Crotalidae venom. Some amino acid residues located in or close to the interfacial binding surface of the group-II basic PLA2s were suggested to be involved in selective binding to PLIβ. PLIγ was a 100-kDa glycoprotein containing 25-kDa and 20-kDa subunits and inhibited all of the PLA2s investigated equally, including Elapidae venom PLA2s (group I), Crotalidae and Viperidae venom PLA2s (group II) and honey-bee PLA2 (group III). From the N-terminal sequences of the two subunits, PLIγ was found to be the same type of PLI that had been purified from Thailand cobra plasma.

Effect of amino acid infusion on renal hemodynamics in humans: a dose-response study

1994 ◽  
Vol 267 (5) ◽  
pp. F703-F708 ◽  
Author(s):  
M. Giordano ◽  
P. Castellino ◽  
E. L. McConnell ◽  
R. A. DeFronzo
Keyword(s):  
Amino Acid ◽  
Dose Response ◽  
Renal Hemodynamics ◽  
Group Iv ◽  
Group V ◽  
Group Iii ◽  
Amino Acid Infusion ◽  
Group I ◽  
Basal Plasma ◽  
Group Ii

We evaluated the dose-response relationship between the plasma amino acid (AA) concentration and renal hemodynamics in eight normal subjects. After an overnight fast, a balanced 10% AA solution was infused for 180 min at five separate infusion rates: 0.5 (group I), 1.0 (group II), 2.0 (group III), 4.0 (group IV), and 6.0 (group V) ml.kg-1.min-1 on separate days. Basal plasma AA concentration was 1.87 +/- 0.1 mmol/l and increased to 2.26 +/- 0.1 (group I), 2.66 +/- 0.2 (group II), 3.79 +/- 0.5 (group III), 5.81 +/- 0.4 (group IV), and 7.41 +/- 0.4 mmol/l (group V). Basal glomerular filtration rate (GFR) and renal plasma flow (RPF) averaged 95 +/- 4 and 476 +/- 29 ml.1.73 m-2.min-1, respectively, and rose to 98 +/- 5 and 506 +/- 40 (group I) [P = not significant (NS)], 102 +/- 3 and 533 +/- 30 (group II) (P < 0.05 vs. basal), 110 +/- 4 and 567 +/- 29 (group III), 115 +/- 7 and 610 +/- 55 (group IV), and 117 +/- 7 and 614 +/- 66 ml.1.73 m-2.min-1 (group V) (P = NS vs. group IV). Basal plasma glucagon concentration averaged 68 +/- 10 pg/ml and increased to 74 +/- 10 (group I), 83 +/- 11 (group II) (P < 0.05 vs. basal), 100 +/- 14 (group III), 121 +/- 14 (group IV), and 229 +/- 35 pg/ml (group V) (P < 0.01 vs. basal). Increases in plasma growth hormone (GH) and insulin levels were observed only during groups IV and V.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Pathomechanism of Insulin Resistance in Men with Central Obesity: Correlation of GGT, GPx, hs-CRP and Plasma Total Cysteine

2013 ◽  
Vol 5 (2) ◽  
pp. 101 ◽  
Author(s):  
Ritawaty Ritawaty ◽  
Indriyanti Rafi Sukmawati ◽  
Ilhamjaya Patellongi ◽  
Ferry Sandra
Keyword(s):  
Oxidative Stress ◽  
Insulin Resistance ◽  
Amino Acid ◽  
Fatty Liver ◽  
Central Obesity ◽  
Group Iv ◽  
Group Iii ◽  
Group I ◽  
Group Ii ◽  
Hs Crp

BACKGROUND: Gamma glutamyltransferase (GGT) was reported recently to be associated with inflammation, oxidative stress and increased amino acid. However, role of GGT in insulin resistance pathomechanism is not exactly known. Therefore correlation of GGT with inflammation, oxidative stress and elevated amino acid, in men with central obesity need to be confirmed.METHODS: A cross-sectional study was designed. Men with central obesity were recruited and selected. Anthropometric parameters, creatinine, hs-CRP, fasting glucose, fasting insulin, glutathione peroxidase (GPx) activity, GGT, plasma total cysteine (tCys) and fatty liver were measured. Subjects were then divided in 4 groups based on waist circumference (WC) and fatty liver: Group I: WC ≤100 cm, without fatty liver; Group II: WC ≤100 cm, with fatty liver; Group III: WC >100 cm, without fatty liver; Group IV: WC >100 cm, with fatty liver. All biochemical characteristics in each group were then statistically analyzed.RESULTS: Seventy-two men with central obesity were selected. Numbers of subjects in each group were: Group I: n=33; Group II: n=5; Group III: n=17; Group IV: n=17. We found significant difference of HOMA-IR between Group I and IV, significant correlation between GGT and HOMAIR, and significant negative correlation between tCys with HOMA-IR in Group IV.CONCLUSION: GGT was significantly correlated with HOMA-IR in men with WC >100 cm and fatty liver. Further investigation with more subjects is necessary to determine clear GGT cut-off to distinguish subjects with fatty liver and insulin resistance.KEYWORDS: GGT, hs-CRP, GPx, tCys, HOMA-IR, insulin resistance

scholarly journals Effect of organic and mineral selenium sources on production performance and selected physiological indicators in swine

2017 ◽  
Vol 73 (12) ◽  
pp. 756-763
Author(s):  
Anna Szuba-Trznadel ◽  
Tomasz Hikawczuk ◽  
Adam Ciura ◽  
Bogusław Fuchs
Keyword(s):  
Amino Acid ◽  
Blood Serum ◽  
Production Performance ◽  
Control Group ◽  
Lactation Period ◽  
Feed Conversion ◽  
Group Iii ◽  
Group I ◽  
Acid Chelate ◽  
Group Ii

The study was conducted on sows (hybrids of wbp × pbz breeds) and their offspring (until day 75 of life) kept on a farm. The aim of the experiment was to compare the effects of different sources of selenium (Se) on the production performance of the animals, Se content in their blood, the level of Se in sow’s colostrum, as well as Gpx, haptoglobin and immunoglobulin levels in the serum of sows and their offspring. Experimental feed mixtures for pregnant sows (LP), lactating sows (LK) and piglets (prestarter and starter) in each treatment had an identical basic composition, differing only in the type of selenium forms. Group I received a mineral form of Se in an amount of 0.2 mg/kg; group II received a mixture of a Se amino acid chelate and the mineral form of Se (0.1 mg/kg of each); group III received a Se amino acid chelate (0.2 mg/kg), and group IV received Se-enriched yeasts (0.2 mg/kg). Beneficial effects of the organic forms of Se were evident already in the lactation period. Sows, especially those from group II receiving 0.2 mg/kg of organic Se, had a higher feed intake, which was related to a higher milk production during lactation. As a result, on the weaning day, piglets from this group were significantly heavier than the other piglets. After weaning, as well, the piglets in this group were significantly heavier. These results were confirmed by parameters of blood serum and whey colostrum. Selenium as a chelate was more available than the mineral and enriched yeast forms. For this reason, the animals receiving the chelate were healthier (fewer inflammations were noted). The animals in this group also showed a better feed conversion compared with the others. The Gpx level in sows’ serum varied depending on the treatment. The highest level of this parameter was determined in sows from group III (receiving 0.2 mg/kg of organic Se), and it differed significantly from its value in the control group. The results showed that the Gpx level was related to the Se concentration in blood serum, which was also confirmed by a higher production of selenocysteine (a part of Gpx). Cells of the animals from this group were better protected against free radicals. Administration of 0.1 mg/kg of organic Se positively affects the performance of animals, but the recommended level in feed is 0.2 mg/kg of a selenium-containing amino acid....

scholarly journals FIBRINOLYTIC AND PROTEOLYTIC ACTIVITY OF BLOOD PLASMA IN PEPTIC ULCER OF THE STOMACH, TAKING INTO ACCOUNT THE PATHOGENIC STRAINS OF HELICOBACTER PYLORI

2020 ◽  
Vol 8 (1) ◽  
pp. 1-7
Author(s):  
L. M. Honcharuk ◽  
O. I. Fediv ◽  
V. T. Kulachek ◽  
Y. M. Teleki
Keyword(s):  
Helicobacter Pylori ◽  
Peptic Ulcer ◽  
Blood Plasma ◽  
Proteolytic Activity ◽  
Fibrinolytic Activity ◽  
Control Group ◽  
Group Iii ◽  
Group I ◽  
Group Ii ◽  
Cag A

The purpose of the study is to investigate changes in fibrinolytic and proteolytic activity of blood plasma in patients with peptic ulcer (PU) taking into account pathogenic Helicobacter pylori (Hp) strains. Materials and methods. 93 patients with PU were examined, of which 30 patients with PU and concomitant Hp cag cag A+/vac A+ (group I), 31 patients with PU and concomitant Hp cag A-/vac A- (group II), 32 patients with PU without concomitant HP infection (group III). The control group consisted of 30 healthy individuals. Fibrinolytic activity of blood plasma was investigated with the help of lysis of azofibrin (fibrin associated with the azo dye orange), which in the alkaline medium turns a bright red color. The level of total (ТFA), enzymatic (FFA) and non-enzymatic fibrinolytic activity (NFA) was evaluated. Proteolytic activity of blood plasma was determined by the lysis of azoalbumin, azocasein and azokol. Research results. The study of fibrinolytic activity of blood plasma showed that the total fibrinolytic activity of blood plasma (TFA) in all groups was significantly higher compared to the control indicators: in patients of group I by 61.5 %, in patients by 40.9 %, in patients of group III by 30.3 %, with a significant intergroup difference between the groups. The growth of TFA was mainly due to FFA. In patients of group I, FFA increased by 2.06 times (p < 0.05), and in patients of group II – by 1.79 times (p < 0.05), in patients of group IIІ – by 1.52 times (p < 0.05) compared with the control. In patients with group I, FFA increased by 12.5 % ​​(p < 0.05) compared with group II. In all patients examined, there was an increase in the proteolytic activity of blood plasma, in particular in group I, the lysis of azoalbumin, azocasein and azocolol increased significantly 2.94 times, 2.83 times and 1.90 times, respectively, and in the patients of group II the investigated indicators increased accordingly 1.87-fold (p < 0.05), 1.96-fold (p < 0.05) and 1.40-fold (p < 0.05), in patients of group III, respectively 1.55 times (p < 0.05), 1.59 times (p < 0.05) and 1.18 times, compared to these values ​​in almost healthy subjects. Significantly more significant changes in proteolysis were detected in the presence of pathogenic Hp strains. Conclusion. Increased proteolytic and fibrinolytic activity of blood plasma is observed in patients with PU. The presence of concomitant Hp in PU leads to more pronounced changes in proteolysis and fibrinolysis. Pathogenic strains of Hp cag cag A+/vac A+ cause significantly more abnormalities in hemostasis.

Characterization of the sulfated glycopeptide of chicken pepsinogen

1982 ◽  
Vol 47 (2) ◽  
pp. 709-718 ◽  
Author(s):  
Miroslav Baudyš ◽  
Vladimír Kostka ◽  
Karel Grüner ◽  
Jan Pohl
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Protein Molecule ◽  
Amino Acid Residues ◽  
Terminal Sequence ◽  
Sugar Moiety ◽  
Pepsinogen A ◽  
Identical Amino Acid Sequence ◽  
High Voltage Electrophoresis

S-sulfonated chicken pepsinogen was digested with TPCK-trypsin; large tryptic peptides, separated on Sephadex G-25 fine, were subjected to additional cleavage with α-chymotrypsin. The hold-up fraction of the chymotryptic digest from the Sephadex G-25 column, was resolved by high voltage electrophoresis. The three most acidic zones contained glycopeptides of identical amino acid sequence Val-Ser-Thr-Asn-Glu-Thr-Val-Tyr, yet differed in the composition of the sugar moiety. These glycopeptides, moreover, bear different numbers of sulfate groups which enabled the resolution of the peptides. The most acidic glycopeptide contains 7 glucosamine residues, 3 mannose residues and 5 sulfate groups, the second one 6 glucosamine residues, 3 mannose residues and 4 sulfate groups and the slowest, minority glycopeptide, 5 glucosamine residues, 2 mannose residues and 2 sulfate groups. The entire sugar moiety is attached to one of the chain viaasparagine. In other experiments the glycopeptides were also isolated from the thermolytic digest of chicken pepsin; their C-terminal sequence was shorter by two amino acid residues. The tentative assignment of the glycopeptides to the amino acid sequence of pepsinogen resulted from the analysis of the limited tryptic digest of the whole protein molecule. Chicken pepsinogen is glycosylated at the site of the chain occupied by a phosphoserine residue in hog pepsinogen A.

scholarly journals Isolation and characterization of β- and γ-caseins from horse milk

1982 ◽  
Vol 203 (1) ◽  
pp. 131-139 ◽  
Author(s):  
S Visser ◽  
R Jenness ◽  
R J Mullin
Keyword(s):  
Room Temperature ◽  
Sodium Dodecyl ◽  
Sulphate Group ◽  
Group Iii ◽  
Isolation And Characterization ◽  
Group I ◽  
Beta Casein ◽  
Group Ii ◽  
Phosphate Groups

Three groups of casein components were isolated from horse milk. Group I is almost insoluble at acid and neutral pH, and is rather heterogeneous on alkaline gels with or without sodium dodecyl sulphate. Group II shows strong similarity to beta-casein from other species, as concluded from its amino acid composition and its N- and C-terminal sequences. This group consists of five electrophoretically distinguishable forms, all containing ester phosphate groups but no carbohydrate. Group III is composed of C-terminal fragments of the beta-like (group II) fraction and probably arises from the action of a plasmin-like enzyme present in horse milk. It does not contain phosphate or carbohydrate. Homology of this group with bovine gamma-caseins is demonstrated. Both beta- and gamma-like caseins are more soluble at 4 degrees C than at room temperature.

Amino acid sequence and biological characterization of BlatPLA2, a non-toxic acidic phospholipase A2 from the venom of the arboreal snake Bothriechis lateralis from Costa Rica

Toxicon ◽  
2013 ◽  
Vol 73 ◽  
pp. 71-80 ◽  
Author(s):  
Marco Van der Laat ◽  
Julián Fernández ◽  
Jordi Durban ◽  
Eva Villalobos ◽  
Erika Camacho ◽  
...  
Keyword(s):  
Amino Acid ◽  
Costa Rica ◽  
Amino Acid Sequence ◽  
Phospholipase A2 ◽  
Biological Characterization

scholarly journals Isolation and properties of lysophospholipases from the venom of an Australian elapid snake, Pseudechis australis

1982 ◽  
Vol 203 (1) ◽  
pp. 269-276 ◽  
Author(s):  
C Takasaki ◽  
N Tamiya
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Phospholipase A2 ◽  
Maximum Activity ◽  
Haemolytic Activity ◽  
Amino Acid Residues ◽  
Terminal Amino Acid ◽  
Optimum Ph ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence

Two lysophospholipases were isolated from the venom of an Australian elapid snake (subfamily Acanthophiinae), Pseudechis australis, by sequential chromatography on CM-52 cellulose, Sephadex G-75 and DE-52 cellulose columns. They were very similar to each other. One of them, lysophospholipase I, was obtained as a homodimer, the monomer of which consisted of 123 amino acid residues with seven disulphide bridges. The amino acid composition and the N-terminal amino acid sequence of the enzyme were similar to those of phospholipase A2, Ca2+ was required for its activity and the maximum activity was attained at 2 mM-CaCl2 in the presence of 1 mM-EDTA. The optimum pH was 7.5. Lysophospholipase I hydrolysed lysophosphatidylcholine more rapidly than lysophosphatidylethanolamine. It did not hydrolyse, however, phosphatidylcholine, 1-palmitoylglycerol, tripalmitoylglycerol or p-nitrophenyl acetate. Modification of the enzyme with p-bromophenacyl bromide or 2-nitrophenylsulphenyl chloride suppressed the activity. A strong direct haemolytic activity was exhibited when the lysophospholipase was present together with phospholipase A2.

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