Biochemical analysis and kinetic modeling of the thermal inactivation of MBP-fused heparinase I: Implications for a comprehensive thermostabilization strategy

2011 ◽  
Vol 108 (8) ◽  
pp. 1841-1851 ◽  
Author(s):  
Shuo Chen ◽  
Fengchun Ye ◽  
Yang Chen ◽  
Yu Chen ◽  
Hongxin Zhao ◽  
...  
Keyword(s):  
Kinetic Modeling ◽  
Biochemical Analysis ◽  
Thermal Inactivation ◽  
Heparinase I

Kinetic modeling of thermal inactivation of antimicrobial peptides produced by Lactobacillus sakei subsp. sakei 2a

2015 ◽  
Vol 605 ◽  
pp. 95-99 ◽  
Author(s):  
Patrícia da Silva Malheiros ◽  
Voltaire Sant ◽  
Adriano Brandelli ◽  
Bernadette Dora Gombossy de Melo Franco
Keyword(s):  
Antimicrobial Peptides ◽  
Kinetic Modeling ◽  
Thermal Inactivation ◽  
Lactobacillus Sakei

Kinetic Modeling of the Thermal Inactivation of Bacteriocin-Like Inhibitory Substance P34

2010 ◽  
Vol 58 (5) ◽  
pp. 3147-3152 ◽  
Author(s):  
Voltaire Sant’Anna ◽  
Michele Utpott ◽  
Florencia Cladera-Olivera ◽  
Adriano Brandelli
Keyword(s):  
Kinetic Modeling ◽  
Thermal Inactivation ◽  
Inhibitory Substance

Mechanism of thermal inactivation of a fusion heparinase I and improvement of its thermostability

2008 ◽  
Vol 136 ◽  
pp. S291
Author(s):  
Shuo Chen ◽  
Fengchun Ye ◽  
Yu Chen ◽  
Ying Kuang ◽  
Yin Chen ◽  
...  
Keyword(s):  
Thermal Inactivation ◽  
Heparinase I

Kinetic modeling of thermal inactivation of the Bacillus sp. protease P7

2012 ◽  
Vol 36 (7) ◽  
pp. 993-998 ◽  
Author(s):  
Voltaire Sant’Anna ◽  
Ana Paula Folmer Corrêa ◽  
Daniel Joner Daroit ◽  
Adriano Brandelli
Keyword(s):  
Kinetic Modeling ◽  
Thermal Inactivation ◽  
Bacillus Sp

Mitochondria in Cardiomyopathy: Alterations in Size, Number and Internal Structures

1968 ◽  
Vol 26 ◽  
pp. 126-127
Author(s):  
George Hug ◽  
William K. Schubert
Keyword(s):  
Heart Failure ◽  
Biochemical Analysis ◽  
Left Ventricular ◽  
Size Number ◽  
Internal Structures ◽  
Left Ventricular Outflow ◽  
Chest X Ray ◽  
Myocardial Fibers ◽  
Muscle Biopsies ◽  
Needle Liver Biopsy

A white boy six months of age was hospitalized with respiratory distress and congestive heart failure. Control of the heart failure was achieved but marked cardiomegaly, moderate hepatomegaly, and minimal muscular weakness persisted.At birth a chest x-ray had been taken because of rapid breathing and jaundice and showed the heart to be of normal size. Clinical studies included: EKG which showed biventricular hypertrophy, needle liver biopsy which showed toxic hepatitis, and cardiac catheterization which showed no obstruction to left ventricular outflow. Liver and muscle biopsies revealed no biochemical or histological evidence of type II glycogexiosis (Pompe's disease). At thoracotomy, 14 milligrams of left ventricular muscle were removed. Total phosphorylase activity in the biopsy specimen was normal by biochemical analysis as was the degree of phosphorylase activation. By light microscopy, vacuoles and fine granules were seen in practically all myocardial fibers. The fibers were not hypertrophic. The endocardium was not thickened excluding endocardial fibroelastosis. Based on these findings, the diagnosis of idiopathic non-obstructive cardiomyopathy was made.

3H-galactose and 3H-glucose incorporation into newly synthesized hepatic glycogen in control-fed rats

1986 ◽  
Vol 44 ◽  
pp. 292-293
Author(s):  
J.E. Michaels ◽  
S.A. Garfield ◽  
J.T. Hung ◽  
S.S. Smith ◽  
R.R. Cardell
Keyword(s):  
Biochemical Analysis ◽  
Glycogen Synthesis ◽  
Hepatic Glycogen ◽  
Electron Microscopic ◽  
Once Daily ◽  
Tail Vein ◽  
Tracer Dose ◽  
Glucose Incorporation ◽  
Wet Weight

3H-galactose (gal) and 3H-glucose (glu) were compared to determine which compound was preferable for pulse labeling newly formed hepatic glycogen. Control fed rats were used to achieve substantial and consistent levels of hepatic glycogen and to stimulate glycogen synthesis.Rats fed once daily for 4 hr achieved hepatic glycogen levels > 3% wet weight liver prior to injection by tail vein of a tracer dose of 3H-gal or 3H-glu. The rats were sacrificed 15-120 min later and liver was prepared by routine techniques for light (LM) and electron microscopic (EM) radioautography (RAG) and biochemical analysis.

Allene oxidation in jet-stirred reactor : a kinetic modeling study

1990 ◽  
Vol 87 ◽  
pp. 1159-1172 ◽  
Author(s):  
P Dagaut ◽  
M Cathonnet ◽  
B Aboussi ◽  
JC Boettner
Keyword(s):  
Kinetic Modeling ◽  
Stirred Reactor ◽  
Allene Oxidation ◽  
Modeling Study

Mechanism of Inhibitory Action on Platelet Activation of a Phospholipase A2 Isolated from Lachesis muta (Bushmaster) Snake Venom

1997 ◽  
Vol 78 (05) ◽  
pp. 1372-1380 ◽  
Author(s):  
André L Fuly ◽  
Olga L T Machado ◽  
Elias W Alves ◽  
Célia R Carlinis
Keyword(s):  
Platelet Aggregation ◽  
Enzymatic Activity ◽  
Phospholipase A2 ◽  
Inhibitory Activity ◽  
Thermal Inactivation ◽  
Anticoagulant Activity ◽  
Gel Filtration ◽  
Apparent Molecular Weight ◽  
Crude Venom ◽  
Lachesis Muta

SummaryCrude venom from Lachesis muta exhibited procoagulant, proteolytic and phospholipase A2 activities. A phospholipase A2, denoted LM-PLA2 was purified from L. muta venom to homogeneity, through a combination of chromatographic steps involving gel-filtration on Sephacryl S-200 HR and reverse phase chromatography on a C2/C18 column. LM-PLA2 presented a single polypeptide chain with an isoelectric point at pH 4.7 and apparent molecular weight of 17 kDa. Partial aminoacid sequence indicated a high degree of homology for LM-PLA2 with other PLA2 from different sources.LM-PLA2 displayed a potent enzymatic activity as measured by indirect hemolysis of red blood cells but it was neither lethal when injected i.p. into mice nor did it present anticoagulant activity. Furthermore, LM-PLA2 displayed a moderate inhibitory activity on the aggregation of rabbit platelets induced by low levels of ADP, thrombin and arachidonate. In contrast, platelet aggregation induced by high doses of collagen was strongly inhibited by LM-PLA2 as well as ATP-release. Treatment of the protein with p-bromophenacyl bromide or 2-mercapto-ethanol, as well as thermal inactivation studies, suggested that the platelet inhibitory effect of LM-PLA2 is dependent on its enzymatic activity. Thus, the platelet inhibitory activity of LM-PLA2 was shown to be dependent on the hydrolysis of plasma phospholipids and/or lipoproteins, most probably those rich in phosphatidylcholine. Surprisingly, lyso-phosphatidylcholine released by LM-PLA2 from plasma was shown to preferentially inhibited collagen-induced platelet aggregation, in contrast to other PLA2s, whose plasma hydrolytic products indistinctly affect platelet’s response to several agonists.

Sign in / Sign up

Export Citation Format

Share Document