VOLUME CHANGES IN PROTEIN REACTIONS .1. IONIZATION REACTIONS OF PROTEINS

[1] THERMODYNAMIC QUANTITIES FOR THE DISSOCIATION EQUILIBRIA OF BIOLOGICALLY IMPORTANT COMPOUNDS .4. 2ND ACID DISSOCIATION OF GLUCOSE 1-PHOSPHORIC ACID [J]. BIOCHEMICAL JOURNAL, 1955, 59 (02) : 203 - 208

[2] THERMODYNAMIC QUANTITIES FOR THE DISSOCIATION EQUILIBRIA OF BIOLOGICALLY IMPORTANT COMPOUNDS .2. THE ACID DISSOCIATIONS OF GLYCEROL 2-PHOSPHORIC ACID [J]. BIOCHEMICAL JOURNAL, 1954, 56 (02) : 198 - 207

[3] THERMODYNAMIC QUANTITIES FOR THE DISSOCIATION EQUILIBRIA OF BIOLOGICALLY IMPORTANT COMPOUNDS .1. THEORY AND EXPERIMENTAL METHOD [J]. BIOCHEMICAL JOURNAL, 1954, 56 (02) : 190 - 196

[4] INCREASE IN ACID-BINDING SITES ON DENATURATION OF HORSE FERRIHEMOGLOBIN AT 0-DEGREES [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1959, 81 (21) : 5679 - 5687

[5] DISTINCT REVERSIBLY DENATURED FERRIHEMOGLOBINS PRODUCED AT PH 3.5 [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1960, 82 (11) : 2756 - 2762

[6] CANNAN R. KEITH, 1941, ANN NEW YORK ACAD SCI, V41, P243, DOI 10.1111/j.1749-6632.1941.tb35241.x

[7] CHARLWOOD PA, 1957, CAN J CHEM, V35, P99

[8] The state of tyrosine in egg albumin and in insulin as determined by spectrophotometric titration [J]. BIOCHEMICAL JOURNAL, 1943, 37 : 302 - 310

[9] ABNORMAL IONIZABLE GROUPS IN LYSOZYME [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1960, 82 (09) : 2154 - 2163

[10] Drude P., 1894, Z PHYS CHEM, V15, P79, DOI [10.1515/zpch-1894-1506, DOI 10.1515/ZPCH-1894-1506]

[1] THERMODYNAMIC QUANTITIES FOR THE DISSOCIATION EQUILIBRIA OF BIOLOGICALLY IMPORTANT COMPOUNDS .4. 2ND ACID DISSOCIATION OF GLUCOSE 1-PHOSPHORIC ACID [J]. BIOCHEMICAL JOURNAL, 1955, 59 (02) : 203 - 208

[2] THERMODYNAMIC QUANTITIES FOR THE DISSOCIATION EQUILIBRIA OF BIOLOGICALLY IMPORTANT COMPOUNDS .2. THE ACID DISSOCIATIONS OF GLYCEROL 2-PHOSPHORIC ACID [J]. BIOCHEMICAL JOURNAL, 1954, 56 (02) : 198 - 207

[3] THERMODYNAMIC QUANTITIES FOR THE DISSOCIATION EQUILIBRIA OF BIOLOGICALLY IMPORTANT COMPOUNDS .1. THEORY AND EXPERIMENTAL METHOD [J]. BIOCHEMICAL JOURNAL, 1954, 56 (02) : 190 - 196

[4] INCREASE IN ACID-BINDING SITES ON DENATURATION OF HORSE FERRIHEMOGLOBIN AT 0-DEGREES [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1959, 81 (21) : 5679 - 5687

[5] DISTINCT REVERSIBLY DENATURED FERRIHEMOGLOBINS PRODUCED AT PH 3.5 [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1960, 82 (11) : 2756 - 2762

[6] CANNAN R. KEITH, 1941, ANN NEW YORK ACAD SCI, V41, P243, DOI 10.1111/j.1749-6632.1941.tb35241.x

[7] CHARLWOOD PA, 1957, CAN J CHEM, V35, P99

[8] The state of tyrosine in egg albumin and in insulin as determined by spectrophotometric titration [J]. BIOCHEMICAL JOURNAL, 1943, 37 : 302 - 310

[9] ABNORMAL IONIZABLE GROUPS IN LYSOZYME [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1960, 82 (09) : 2154 - 2163

[10] Drude P., 1894, Z PHYS CHEM, V15, P79, DOI [10.1515/zpch-1894-1506, DOI 10.1515/ZPCH-1894-1506]