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56 1 Amino Acids, Peptides, Proteins

Fig. 1.28. Tertiary structures (schematic: spiral: α-helix, arrow: pleated sheet) of the β-chain of hemoglobin (a),

of triosephosphate isomerase (b) and carboxypeptidase (c). (according to Walton, 1981)

However, a PrPp forces the pathogenic conformation

on a PrPn. The stability towards serine

proteinase K from the fungus Tritirachium

album is used to differentiate between PrPp

and PrPn. Serine proteinase K, which attacks

the carboxyl side of hydrophobic amino acids,

largely hydrolyzes PrPn while a characteristic

peptide (M r 27-30 kDa) is released from PrPp.

This marker can be identified using the sandwich

ELISA (cf. 2.6.3).

1.4.2.3.4 Quaternary Structures

In addition to the free energy gain by folding

of a single peptide chain, association of more

than one peptide chain (subunit) can provide

further gains in free energy. For example,

hemoglobin (4 associated peptide chains)

G 0 = −46 kJ mole −1 and the trypsin-trypsin

inhibitor complex (association of 2 peptide

chains) G 0 = − 75.2kJmole −1 . In principle

such associations correspond to the folding of

a larger peptide chain with several structural

domains without covalently binding the subunits.

Table 1.26 lists some proteins which partially

exhibit quaternary structures.

1.4.2.4 Denaturation

The term denaturation denotes a reversible or irreversible

change of native conformation (tertiary

structure) without cleavage of covalent bonds (except

for disulfide bridges). Denaturation is possible

with any treatment that cleaves hydrogen

Table 1.26. Examples of globular proteins

Name Origin Molecular Number

weight of

(Kdal) subunits

Lysozyme Chicken egg 14.6 1

Papain Papaya latex 20.7 1

α-Chymotrypsin Pancreas 23 1

(beef)

Trypsin Pancreas 23.8 1

(beef)

Pectinesterase Tomato 27.5

Chymosin Stomach 31

(calf)

β-Lactoglobulin Milk 35 2

Pepsin A Stomach 35 1

(swine)

Peroxidase Horseradish 40 1

Hemoglobin Blood 64.5 4

Avidin Chicken egg 68.3 4

Alcoholdehydrogenase

Liver (horse) 80 2

Yeast 150 4

Hexokinase Yeast 104 2

Lactate

dehydrogenase Heart (swine) 135 4

Glucose oxidase P. notatum 152

Pyruvate kinase Yeast 161 8

A. niger 186

β-Amylase Sweet potato 215 4

Catalase Liver (beef) 232 4

M. lysodeikticus 232

Adenosine

triphosphatase Heart (beef) 284 6

Urease Jack beans 483 6

Glutamine

synthetase E. coli 592 12

Arginine

decarboxylase E. coli 820 10

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