Biochemical basis for the differences in plant protein utilization

1974 ◽  
Vol 22 (4) ◽  
pp. 550-555 ◽  
Author(s):  
Madhusudan L. Kakade
Keyword(s):  
Plant Protein ◽  
Protein Utilization ◽  
Biochemical Basis

scholarly journals Nutritional programming improves dietary plant protein utilization in zebrafish Danio rerio

PLoS ONE ◽  
2020 ◽  
Vol 15 (3) ◽  
pp. e0225917 ◽  
Author(s):  
Karolina Kwasek ◽  
Michal Wojno ◽  
Federica Iannini ◽  
Vance J. McCracken ◽  
Giovanni S. Molinari ◽  
...  
Keyword(s):  
Danio Rerio ◽  
Plant Protein ◽  
Protein Utilization ◽  
Nutritional Programming

Protein utilization by young women consuming animal or plant protein diets at various levels of vitamin B-6 intake

1989 ◽  
Vol 49 (4) ◽  
pp. 636-640 ◽  
Author(s):  
C A Hudson ◽  
A A Betschart ◽  
J R Turnlund ◽  
M J Kretsch ◽  
H E Sauberlich
Keyword(s):  
Young Women ◽  
Plant Protein ◽  
Vitamin B ◽  
Protein Utilization ◽  
Protein Diets

Dietary plant protein utilization in Atlantic cod, Gadus morhua L.

2007 ◽  
Vol 13 (3) ◽  
pp. 200-215 ◽  
Author(s):  
A.-C. HANSEN ◽  
Ø. KARLSEN ◽  
G. ROSENLUND ◽  
M. RIMBACH ◽  
G.-I. HEMRE
Keyword(s):  
Gadus Morhua ◽  
Atlantic Cod ◽  
Plant Protein ◽  
Protein Utilization

Synergistic interaction of triterpenoid saponins and plant protein toxins

Planta Medica ◽  
2012 ◽  
Vol 78 (11) ◽  
Author(s):  
A Weng ◽  
M Thakur ◽  
F Beceren-Braun ◽  
R Gilabert-Oriol ◽  
S Boettger ◽  
...  
Keyword(s):  
Synergistic Interaction ◽  
Plant Protein ◽  
Triterpenoid Saponins ◽  
Protein Toxins

Enhancement of Plasminogen Binding to U937 Cells and Fibrin by Complestatin

1997 ◽  
Vol 77 (01) ◽  
pp. 137-142 ◽  
Author(s):  
Kiyoshi Tachikawa ◽  
Keiji Hasurni ◽  
Akira Endo
Keyword(s):  
Binding Site ◽  
Binding Affinity ◽  
Blood Cells ◽  
Aminocaproic Acid ◽  
U937 Cells ◽  
Biochemical Basis ◽  
Equilibrium Binding ◽  
Pharmacological Stimulation ◽  
Endogenous Fibrinolysis ◽  
Stimulation Of

SummaryPlasminogen binds to endothelial and blood cells as well as to fibrin, where the zymogen is efficiently activated and protected from inhibition by α2-antiplasmin. In the present study we have found that complestatin, a peptide-like metabolite of a streptomyces, enhances binding of plasminogen to cells and fibrin. Complestatin, at concentrations ranging from 1 to 5 μM, doubled 125I-plasminogen binding to U937 cells both in the absence and presence of lipoprotein(a), a putative physiological competitor of plasminogen. The binding of 125I-plasminogen in the presence of complestatin was abolished by e-aminocaproic acid, suggesting that the lysine binding site(s) of the plasminogen molecule are involved in the binding. Equilibrium binding analyses indicated that complestatin increased the maximum binding of 125I-plasminogen to U937 cells without affecting the binding affinity. Complestatin was also effective in increasing 125I-plasminogen binding to fibrin, causing 2-fold elevation of the binding at ~1 μM. Along with the potentiation of plasminogen binding, complestatin enhanced plasmin formation, and thereby increased fibrinolysis. These results would provide a biochemical basis for a pharmacological stimulation of endogenous fibrinolysis through a promotion of plasminogen binding to cells and fibrin.

Biochemical basis of selective disease controlling activity of mepanipyrim

2007 ◽  
Vol 32 (2) ◽  
pp. 77-82 ◽  
Author(s):  
Ichiro Miura ◽  
Shinichiro Maeno
Keyword(s):  
Biochemical Basis

Penggunaan Standar Bumbu Masakan Lauk Hewani dan Nabati di RSUD Panembahan Senopati Bantul Yogyakarta

2017 ◽  
Vol 19 (2) ◽  
pp. 131-139
Author(s):  
Kukuh Probo Sukmawati ◽  
Setyowati Setyowati ◽  
Th Ninuk Sri Hartini
Keyword(s):  
Animal Protein ◽  
Plant Protein ◽  
Observational Research ◽  
Plant Proteins ◽  
Tabular Form ◽  
Cross Sectional ◽  
Herbs And Spices

  Background: Using of herbs and spices greatly affect the taste of foods, although the ingredients used are the same, different formulations of herbs will produce different flavors. Standardized seasonings are needed to produce a relatively similar food taste. Objective: The research aims to determine the use of herbs in animal and plant proteins. Method: This research was an observational research with cross sectional approach at PanembahanSenopati Hospital Bantul. The objects of this research were standardized seasonings inanimal and plant proteinsin the menu cycle of 10 days in Juny 2015. The data were analyzed descriptively and presented in tabular form and textural. Result: Standardized Seasonings in animal protein were B for satay and C for semur. Standardized seasonings in plant protein were B for bali, terik, rujak and D for bacem. The percentage of the use of seasoning than standardized seasoning for satay (148,7%), bali (130,3%), rujak(372%),for semur, terik and bacem the conformity are not not known because the standardized seasonings unwritten. The conformity of ingredient herbskind for satay (66,7%), semur (100%), bali (54,5%), rujak (50%), bacem (100%) and terik (100%). Conclusion:The conformity of herbs weight foranimal protein (124,3%) and plant protein (175,5%). The conformity of ingredient herbskind for animal protein (83,3%) and plant protein (76,1%). Standardized seasonings used were B, C and D.   Keywords: standardized seasonings, animal protein, plant protein

Effective Utilization of Soybean Curd Residue for Chicken Feed as a Plant Protein Source.

1999 ◽  
Vol 36 (5) ◽  
pp. 311-318 ◽  
Author(s):  
Prapakorn TARACHAI ◽  
Narin THONGWITTAYA ◽  
Hiroshi KAMISOYAMA ◽  
Koh-en YAMAUCHI
Keyword(s):  
Protein Source ◽  
Plant Protein ◽  
Effective Utilization ◽  
Soybean Curd ◽  
Soybean Curd Residue
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