isoleucine and egg white

isoleucine has been researched along with egg white in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	2 (100.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	0 (0.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Feinstein, G; Gertler, A	1
Kowalski, D; Laskowski, M	1

Other Studies

2 other study(ies) available for isoleucine and egg white

Article	Year
The effect of limited proteolysis of chicken ovoinhibitor by bovine chymotrypsin on the inhibitory activities against trypsin, chymotrypsin and elastase. European journal of biochemistry, 1972, Nov-21, Volume: 31, Issue:1 Topics: Amino Acids; Animals; Binding Sites; Carboxypeptidases; Cattle; Chemical Phenomena; Chemistry; Chickens; Chromatography, Affinity; Chymotrypsin; Egg Proteins; Egg White; Female; Hydrogen-Ion Concentration; Isoleucine; Ovum; Pancreatic Elastase; Swine; Trypsin Inhibitors; Tyrosine	1972
Inactivation of enzymatically modified trypsin inhibitors upon chemical modification of the -amino group in the reactive site. Biochemistry, 1972, Aug-29, Volume: 11, Issue:18 Topics: Animals; Arginine; Benzoates; Binding Sites; Cattle; Chemical Phenomena; Chemistry; Cyanates; Egg White; Electrophoresis, Disc; Glycine max; Guanidines; Isoleucine; Kinetics; Maleates; Mathematics; Methylation; Mucoproteins; Nitrophenols; Pancreatic Juice; Spectrophotometry; Sulfhydryl Reagents; Swine; Trypsin; Trypsin Inhibitors	1972

Article

Year

The effect of limited proteolysis of chicken ovoinhibitor by bovine chymotrypsin on the inhibitory activities against trypsin, chymotrypsin and elastase.

European journal of biochemistry, 1972, Nov-21, Volume: 31, Issue:1

Topics: Amino Acids; Animals; Binding Sites; Carboxypeptidases; Cattle; Chemical Phenomena; Chemistry; Chickens; Chromatography, Affinity; Chymotrypsin; Egg Proteins; Egg White; Female; Hydrogen-Ion Concentration; Isoleucine; Ovum; Pancreatic Elastase; Swine; Trypsin Inhibitors; Tyrosine

1972

Inactivation of enzymatically modified trypsin inhibitors upon chemical modification of the -amino group in the reactive site.

Biochemistry, 1972, Aug-29, Volume: 11, Issue:18

Topics: Animals; Arginine; Benzoates; Binding Sites; Cattle; Chemical Phenomena; Chemistry; Cyanates; Egg White; Electrophoresis, Disc; Glycine max; Guanidines; Isoleucine; Kinetics; Maleates; Mathematics; Methylation; Mucoproteins; Nitrophenols; Pancreatic Juice; Spectrophotometry; Sulfhydryl Reagents; Swine; Trypsin; Trypsin Inhibitors

1972