Tryptic hydrolysis of bovine αS2-casein: identification and release kinetics of peptides

We have used ribonuclease T1 and its chemically modified derivatives as substrates, and trypsin as proteinase, to investigate the kinetics of proteolysis of a specific peptide bond in the folded and unfolded conformations of a protein. Steady-state kinetic studies showed that Km = 0.27 mM and Kcat. = 2.45 s-1 for the tryptic hydrolysis of the Arg(77)-Val(78) peptide bond in unfolded ribonuclease T1. This Km is somewhat lower than, and the kcat. value similar to, values found for the tryptic hydrolysis of comparable bonds in small peptides. Our data for the initial velocity of hydrolysis of the Arg(77)-Val(78) bond in a solution of the folded protein indicate that the bond is at least 1700 times less rapidly hydrolysed in the folded than in the unfolded conformation of ribonuclease T1, and do not exclude the possibility that the bond is completely resistant to hydrolysis in the folded protein.

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Kinetics of heme octapeptide (microperoxidase-8; MP-8) formation studied by high-pressure liquid chromotography (HPLC) monitoring of the peptic and tryptic hydrolysis of horse heart cytochrome-c

Journal of Inorganic Biochemistry ◽

10.1016/0162-0134(89)80029-7 ◽

1989 ◽

Vol 37 (1) ◽

pp. 55-59 ◽

Cited By ~ 6

Author(s):

Paul A. Adams ◽

Mark P. Byfield ◽

Richard D. Goold ◽

Alfred E. Thumser

Keyword(s):

High Pressure ◽

Cytochrome C ◽

Horse Heart Cytochrome ◽

Horse Heart Cytochrome C ◽

Kinetics Of ◽

Hydrolysis Of ◽

Microperoxidase 8 ◽

Tryptic Hydrolysis

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Release kinetics of Tilapia scale collagen I peptides during tryptic hydrolysis

Food Hydrocolloids ◽

10.1016/j.foodhyd.2017.11.040 ◽

2018 ◽

Vol 77 ◽

pp. 931-936 ◽

Cited By ~ 7

Author(s):

Junde Chen ◽

Long Li ◽

Ruizao Yi ◽

Ran Gao ◽

Jianlin He

Keyword(s):

Release Kinetics ◽

Collagen I ◽

Tilapia Scale ◽

Kinetics Of ◽

Tryptic Hydrolysis

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Kinetics of the Tryptic Hydrolysis of Zinc-free Bovine Insulin

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)63596-3 ◽

1969 ◽

Vol 244 (20) ◽

pp. 5537-5543

Author(s):

Su-Sun Wang ◽

Frederick H. Carpenter

Keyword(s):

Bovine Insulin ◽

Kinetics Of ◽

Hydrolysis Of ◽

Tryptic Hydrolysis

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THE KINETICS OF ENZYME REACTIONS: SCHÜTZ'S LAW

The Journal of General Physiology ◽

10.1085/jgp.13.3.323 ◽

1930 ◽

Vol 13 (3) ◽

pp. 323-334 ◽

Cited By ~ 4

Author(s):

E. A. Moelwyn-Hughes ◽

J. Pace ◽

W. C. M. Lewis

Keyword(s):

Experimental Results ◽

Mass Action ◽

Law Of Mass Action ◽

Enzyme Reactions ◽

Adsorption Theory ◽

The Law ◽

Kinetics Of ◽

Hydrolysis Of ◽

Tryptic Hydrolysis ◽

Made In

1. A review of the applicability of Schütz's Law to enzymic reactions is given. 2. The theoretical deductions of the Law, (a) on the basis of the law of mass action, (b) on the basis of the adsorption theory, are given and the significance of the assumptions made in these deductions pointed out. 3. It is shown that the true critical increment for an enzymic reaction is equal to twice the critical increment calculated from the Schütz constant ks, if the heat of decomposition of the enzyme-products complex be neglected. 4. Experiments are described on the tryptic hydrolysis of casein at 30°C. and 404C. The foregoing considerations are applied to the experimental results obtained.

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