scholarly journals Application of Pressurized Solvents for Ultrafast Trypsin Hydrolysis in Proteomics: Proteomics on the Fly

2008 ◽  
Vol 7 (8) ◽  
pp. 3276-3281 ◽  
Author(s):  
Daniel López-Ferrer ◽  
Konstantinos Petritis ◽  
Kim K. Hixson ◽  
Tyler H. Heibeck ◽  
Ronald J. Moore ◽  
...  
Keyword(s):  
Trypsin Hydrolysis

Effect of Trypsin on Antioxidant Activity and Gel-Rheology of Flaxseed Protein

2017 ◽  
Vol 13 (3) ◽  
Author(s):  
Yuan-yuan Chang ◽  
Chong-hao Bi ◽  
Li-jun Wang ◽  
Dong Li ◽  
Benu Adhikari ◽  
...  
Keyword(s):  
Gel Strength ◽  
Protein Hydrolysates ◽  
Hydrodynamic Diameter ◽  
Considerable Decrease ◽  
Antioxidative Properties ◽  
Trypsin Hydrolysis ◽  
Gelling Property ◽  
High Degree ◽  
Hydrolysis Of ◽  
Antioxidative Property

Abstract Enzymatic hydrolysis of flaxseed protein (FP) was carried out using trypsin in order to obtain flaxseed protein hydrolysates possessing better antioxidative property and modified rheological properties. The antioxidative properties of hydrolysates were much higher than the unhydrolyzed flaxseed protein. The hydrolysis also significantly reduced the hydrodynamic diameter of the magnitude of zeta potential of the dispersions. The gelling point of the hydrolysates occurred earlier than the unhydrolyzed sample while the duration of hydrolysis (30–120 min) did not affect gelling point of the hydrolysates. Considerable decrease in the gel strength and the frequency dependence of gel strength were observed in gels produced using hydrolyzed flaxseed protein. The above findings indicate that hydrolysates possessing high degree of antioxidative properties. The gels produces from these hydrolysates will have fast gelling property and will produce gels with reasonable strength. Thus, flaxseed protein hydrolysates obtained from trypsin hydrolysis can be used in applications that require proteins with higher antioxidative properties but softer texture.

Anterior midgut proteinase inhibitor from Glossina morsitans morsitans Westwood (Diptera: Glossinidae) and its effects upon tsetse digestive enzymes

1980 ◽  
Vol 58 (1) ◽  
pp. 79-87 ◽  
Author(s):  
Jon G. Houseman
Keyword(s):  
Proteinase Inhibitor ◽  
Periplaneta Americana ◽  
Specific Activity ◽  
Glossina Morsitans Morsitans ◽  
Tsetse Flies ◽  
Trypsin Activity ◽  
Glossina Morsitans ◽  
Trypsin Hydrolysis ◽  
Hydrolysis Of ◽  
Anterior Midgut

The anterior midgut of Glossina morsitans morsitans Westwood contains a proteinase inhibitor, molecular weight 5000 ± 2000daltons, stable to 1 M HCl, heat, and dialysis, but unstable to 1% trichloroacetic acid. Inhibitor activity is not associated with anticoagulant in the anterior midgut. The specific activity of the proteinase inhibitor is similar in mated and unmated females and greater than in male tsetse flies. Proteinase inhibitor inhibits proteinase VI and trypsin hydrolysis of N-benzoyl-L-arginine ethyl ester (BAEE) and benzoyl-DL-arginine-p-nitroanilide (BAPNA) but has no effect on proteinase VI hydrolysis of haemoglobin. Inhibition of trypsin hydrolysis of haemoglobin is noncompetitive. Proteinase inhibitor levels in the anterior midgut decreased immediately after feeding and then increased, reaching a maximum 60–100 h after ingestion of the bloodmeal. Postteneral flies contained higher levels of proteinase inhibitor than teneral individuals. Trypsin activity in gut homogenates of Phormia regina and Aedes aegypti was inhibited by the tsetse inhibitor. There was no detectable inhibition of bovine or Pterostichus adstrictus trypsin activity. Inhibition of Periplaneta americana trypsin occurred but was less than fly trypsin inhibition. The possible role of the inhibitor in terminating proteinase production is discussed.

Isolation and characterization of anti-inflammatory peptides derived from trypsin hydrolysis of microalgae protein (Synechococcus sp. VDW)

2019 ◽  
Vol 33 (4) ◽  
pp. 303-324 ◽  
Author(s):  
Rutairat Suttisuwan ◽  
Saranya Phunpruch ◽  
Tanatorn Saisavoey ◽  
Papassara Sangtanoo ◽  
Nuttha Thongchul ◽  
...  
Keyword(s):  
Isolation And Characterization ◽  
Trypsin Hydrolysis ◽  
Synechococcus Sp ◽  
Anti Inflammatory ◽  
Hydrolysis Of

Enzyme-Mediated Self-Assembly of Highly Ordered Structures From Disordered Proteins

2008 ◽  
Author(s):  
Ahmad Athamneh ◽  
Justin Barone
Keyword(s):  
Self Assembly ◽  
Amyloid Fibrils ◽  
Prion Diseases ◽  
Wheat Gluten ◽  
Disordered Proteins ◽  
X Ray Diffraction ◽  
Ordered Structures ◽  
Wide Range ◽  
Trypsin Hydrolysis ◽  
Hydrolysis Of

Trypsin hydrolysis of wheat gluten produced glutamine-rich short peptides with a tendency to self-assemble into supermolecular structures extrinsic to native wheat gluten. Fourier transform infrared and X-ray diffraction data suggested that the new structures formed resembled that of cross-β amyloid fibrils found in some insect silk and implicated in prion diseases. The superstructures were about 10 μm in diameter with clear right-handed helical configuration and appeared to be bundles of smaller fibrils of about 63 nm in diameter. Results demonstrate the potential for utilizing cheap protein sources and natural mechanisms of protein self-assembly to design advanced nanomaterials that can provide a wide range of structural and chemical functionality.

Membrane Glycoproteins of Human and Rabbit Platelets: Studies In Vitro and after Circulation in Vivo

1975 ◽  
Author(s):  
J. N. George ◽  
P. C. Lewis ◽  
D. A. Sears
Keyword(s):  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Age Distribution ◽  
Human Platelets ◽  
Membrane Glycoproteins ◽  
Rabbit Platelets ◽  
Trypsin Hydrolysis ◽  
Initial Recovery

The initial events of hemostasis and thrombosis involve platelet contact interactions and may be mediated by surface glycoproteins. Human and rabbit platelets were labeled with 125I-diazotized diiodosulfanilic acid (I), which reacts covalently with proteins, and proteins were separated by SDS-polyacrylamide gel electrophoresis. Only exposed membrane proteins were labeled because: 1) protein specific activity of membranes was 4-7 times that of whole platelets, 2) different proteins were labeled when I was reacted with isolated membranes, and 3) trypsin-hydrolysis of labeled intact platelets altered the radioactive peaks. Like Phillips (Biochem. 11, 4582, 72) and Nachman et al. (JBC 248, 2928, 73) we found that lactoperoxidase iodinated the 93,000 dalton glycoprotein (GP) of human platelets. In contrast, I labeled both the 93,000 and 118,000 dalton membrane GP of human platelets, and all 3 membrane GP of rabbit platelets.Rabbit platelets labeled simultaneously with I and 51Cr had identical density and therefore age distribution of the 2 labels. After infusion into rabbits, initial recovery of I was 23% of the Cr recovery. After 3 hrs, I disappearance was exponential and more rapid (T/2 = 17 hrs) than the linear Cr disappearance (T/2 = 30 hrs, p < .01). This was due to in vivo removal of I from circulating platelets since 1 did not elute more rapidly from platelets harvested after 3 hrs circulation and incubated in plasma at 37° (T/2 of I elution = 43 hrs, Cr = 33 hrs). Platelets harvested after 14-20 hrs circulation had the same distribution of I on the membrane GP as before circulation. We postulate that this symmetrical label loss indicates uniform loss of membrane GP, suggesting that platelets lose pieces of their plasma membrane during circulation. This could occur during contact interaction in the process of hemostasis.

scholarly journals PREPARATION AND CHARACTERIZATION OF AN IMMUNOELECTRON MICROSCOPE TRACER CONSISTING OF A HEME-OCTAPEPTIDE COUPLED TO Fab

1974 ◽  
Vol 139 (1) ◽  
pp. 208-223 ◽  
Author(s):  
J. P. Kraehenbuhl ◽  
R. E. Galardy ◽  
J. D. Jamieson
Keyword(s):  
Molecular Weight ◽  
Gel Filtration ◽  
Antibody Fragments ◽  
Amino Groups ◽  
Electron Microscope Level ◽  
Ph Optimum ◽  
Peroxidatic Activity ◽  
Stokes Radius ◽  
Trypsin Hydrolysis

A heme-octapeptide (mol wt 1,550) has been obtained from cytochrome c by successive pepsin and trypsin hydrolysis and purified by gel filtration and countercurrent distribution. It possesses peroxidatic activity characterized by an apparent Km of 0.2 M, an apparent vmax of 4 mmol/min per mg of peptide, and a pH optimum of 7.0. Using a novel two-step conjugation procedure, the heme-octapeptide was coupled to rabbit Fab antibody fragments by first derivatizing it with the N-hydroxysuccinimide ester of p-formylbenzoic acid and subsequently allowing it to form a Schiff base with the amino groups of Fab. Stable covalent linkages were then obtained by reduction of the Schiff bases with sodium borohydride. The conjugate consists of ∼2 heme-octapeptides attached to each Fab molecule. The molecular weight is 45,000 daltons when coupled to sheep Fab and 50,000 daltons with a Stokes radius of 32 Å, when conjugated to rabbit Fab. Its peroxidatic activity is characterized by an apparent Km of 0.4 M, an apparent vmax of 0.4 mmol/min and per mg of attached heme-octapeptide and a pH optimum of 7.0. The conjugate has been used for the localization at the electron microscope level of secretory immunoglobulins in the mammary gland of lactating rabbits.

Trypsin Hydrolysis of Lysine Ethyl Ester

1951 ◽  
Vol 73 (3) ◽  
pp. 1382-1382 ◽  
Author(s):  
Harold Werbin ◽  
Ann Palm
Keyword(s):  
Ethyl Ester ◽  
Trypsin Hydrolysis ◽  
Hydrolysis Of

Effects of chelating agents on radioiron absorption and distribution in rats in vivo

1963 ◽  
Vol 205 (5) ◽  
pp. 885-889 ◽  
Author(s):  
J. M. Hopping ◽  
W. S. Ruliffson
Keyword(s):  
Urinary Excretion ◽  
Chelating Agents ◽  
Iron Absorption ◽  
Long Bones ◽  
Iron Chelate ◽  
Trypsin Hydrolysis ◽  
Loop Technique ◽  
Pass Through ◽  
Access To Food

Effects of ethylenediaminetetraacetate (EDTA), citrate, ascorbate, succinate, and sorbitol on the absorption and postabsorptive distribution of Fe59Cl3 in the rat were studied, using an isolated loop technique. Citrate most effectively promoted iron absorption, with ascorbate, EDTA, and succinate following in that order. Sorbitol seemed without effect. Control animals with access to food until time of experiment absorbed more radioiron than did fasted controls. Partial trypsin hydrolysis permitted demonstration that succinate-exposed gut cells most avidly retained iron, while EDTA led to least cellular retention. Postabsorptive distribution among blood, liver, spleen, long bones, kidneys, and urine was unremarkable except that EDTA promoted marked radioiron urinary excretion. EDTA may pass through the gut wall as an intact iron chelate. A pattern of actions during iron absorption is proposed for EDTA, citrate, ascorbate, and succinate.

Sign in / Sign up

Export Citation Format

Share Document