Collection of Czechoslovak Chemical Communications - digital archive 

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• BAUDYŠ M., KOSTKA V., GRÜNER K., HAUSDORF G., HÖHNE W.E.: Amino acid sequence of the small cyanogen bromide peptide of thermitase, a thermostable serine proteinase from Thermoactinomyces vulgaris. International Journal of Peptide and Protein Research 1982, 19, 32. <https://doi.org/10.1111/j.1399-3011.1982.tb03020.x>
• Emöd I., Tong N.-T., Keil B.: Chemical characterization of the homogeneous collagenase from Clostridium histolyticum. Biochimica et Biophysica Acta (BBA) - Enzymology 1981, 659, 283. <https://doi.org/10.1016/0005-2744(81)90054-1>
• Sikorski M.M., Cǎerná J., Rychlík I., Legocki A.B.: Peptidyl transferase activity in wheat germ ribosomes. Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis 1977, 475, 123. <https://doi.org/10.1016/0005-2787(77)90346-X>
• Kušnír Jaroslav, Meloun Bedřich: Sequence of 36 amino acid residues between the 1st and 2nd methionine of human plasma albumin. Biochimica et Biophysica Acta (BBA) - Protein Structure 1973, 310, 124. <https://doi.org/10.1016/0005-2795(73)90015-9>
• Zikán Jiří, Claude Bennett J.: Cyanogen bromide splitting of human immunoglobulin M. Biochimica et Biophysica Acta (BBA) - Protein Structure 1973, 317, 447. <https://doi.org/10.1016/0005-2795(73)90237-7>
• 2′(3′)‐O‐N‐formylmethionyl)‐adenosine‐5′‐phosphate, a new donor substrate in peptidyl transferase catalyzed reactions. FEBS Letters 1973, 37, 188. <https://doi.org/10.1016/0014-5793(73)80455-7>
• Zikán Jiří: J chain in pig immunoglobulins. Immunochemistry 1973, 10, 351. <https://doi.org/10.1016/0019-2791(73)90083-9>
• Prusík Z., Štěpánek J.: Apparatus and methods for horizontal high-voltage electrophoresis on paper with unilateral cooling, operating up to 170 V·cm−1 and 0.6 W·cm−2. Journal of Chromatography A 1973, 87, 73. <https://doi.org/10.1016/S0021-9673(01)91520-1>
• Turková J., Mikeš O., Hayashi K., Danno G., Polgár L.: Alkaline proteinases of the genus aspergillus. Biochimica et Biophysica Acta (BBA) - Protein Structure 1972, 257, 257. <https://doi.org/10.1016/0005-2795(72)90277-2>
• Meloun Bedřich, Kušnír Jaroslav: Amino acid sequence of 37 residues at the carboxyl—terminal end of human plasma albumin. FEBS Letters 1972, 27, 121. <https://doi.org/10.1016/0014-5793(72)80423-X>
• Trufanov V. A., Pshenichnaya E. V., Kozarenko T. D.: Tuberculin-active fragments of mycobacteria of the strain Vallee-58. Chem Nat Compd 1971, 7, 370. <https://doi.org/10.1007/BF00569033>
• Trufanov V. A., Pugacheva N. N., Kozarenko T. D.: A study of a tuberculin-active peptide from mycobacteria of strain Vallee-58. Chem Nat Compd 1971, 7, 372. <https://doi.org/10.1007/BF00569034>
• Kiso Yoshiyuki, Falk Erika: The theoretical study of the paper electrophoretic separation of low molecular weight substances. Journal of Chromatography A 1971, 59, 401. <https://doi.org/10.1016/S0021-9673(01)82232-9>
• Turková J., Mikeś O.: Specificity of alkaline proteinase of Aspergillus flavus. Biochimica et Biophysica Acta (BBA) - Enzymology 1970, 198, 386. <https://doi.org/10.1016/0005-2744(70)90071-9>
• Černá Jiřina, Rychlík Ivan, Žemlička Jiří, Chládek Stanislav: Substrate specificity of ribosomal peptidyl transferase. II. 2′(3′)-O-Aminoacyl nucleosides as acceptors of the peptide chain in the fragment reaction. Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis 1970, 204, 203. <https://doi.org/10.1016/0005-2787(70)90503-4>
• Tomášek V., Šorm F., Zwilling R., Pfleiderer G.: Serine‐containing active center of the trypsin‐like protease of crayfish Astacus leptodactylus. FEBS Letters 1970, 6, 229. <https://doi.org/10.1016/0014-5793(70)80064-3>
• Tomášek V., Strmeň J., Šorm F.: Aspartic acid residue no. 177 of bovine trypsinogen. FEBS Letters 1970, 8, 176. <https://doi.org/10.1016/0014-5793(70)80257-5>
• Novotny Jiri, Franek Frantisek, Sorm Frantisek: Large Scale Isolation, Characterization and Classification of Pig Immunoglobulin k-Chains. Eur J Biochem 1970, 14, 309. <https://doi.org/10.1111/j.1432-1033.1970.tb00291.x>
• Kostka V., Morávek L., ŠOrm F.: Amino Acid Sequence of C‐Terminal Fragment of Hog Pepsin. European Journal of Biochemistry 1970, 13, 447. <https://doi.org/10.1111/j.1432-1033.1970.tb00948.x>
• Rychlík Ivan, ČErná Jiřina, Chládek Stanislav, Pulkrábek Petr, ŽEmlička Jiří: Substrate Specificity of Ribosomal Peptidyl Transferase. European Journal of Biochemistry 1970, 16, 136. <https://doi.org/10.1111/j.1432-1033.1970.tb01064.x>
• Novotný Jiří, Franěk František, ŠOrm František: Study on a Family of Cystine‐Containing Fragments from the Variable Part of Pig Immunoglobulin k‐Chains. European Journal of Biochemistry 1970, 16, 278. <https://doi.org/10.1111/j.1432-1033.1970.tb01082.x>
• Holeyšovský V., Keil B., Sǒrm F.: Location of reactive tyrosine residues in trypsin. FEBS Letters 1969, 3, 107. <https://doi.org/10.1016/0014-5793(69)80109-2>
• Rychlík Ivan, Černá Jiřina, Chládek Stanislav, Žemlička Jiří, Haladová Zuzana: Substrate specificity of ribosomal peptidyl transferase: 2′(3′)-O-aminoacyl nucleosides as acceptors of the peptide chain on the amino acid site. Journal of Molecular Biology 1969, 43, 13. <https://doi.org/10.1016/0022-2836(69)90075-8>
• Novotý J., Franěk F.: N‐ and C‐terminal sequences in pig immunoglobulin π‐chains: Assignment to the K type. FEBS Letters 1968, 2, 93. <https://doi.org/10.1016/0014-5793(68)80111-5>
• Franěk F., Keil B., Nvotný J., ŠOrm F.: Amino Acid Sequence around Disulfide Bridge of Pig Immunoglobin λ‐Chains. European Journal of Biochemistry 1968, 3, 422. <https://doi.org/10.1111/j.1432-1033.1967.tb19548.x>
• MELOUN B., FRIČ I., ŠORM F.: Nitration of Tyrosine Residues in the Pancreatic Trypsin Inhibitor with Tetranitromethane. European Journal of Biochemistry 1968, 4, 112. <https://doi.org/10.1111/j.1432-1033.1968.tb00180.x>
• Zikán J., Škárová B., Rejnek J.: Two structurally different types of rabbit light chains. Folia Microbiol 1967, 12, 162. <https://doi.org/10.1007/BF02896878>
• Jokl V., Majer J., Scharf H., Kroll H.: Papierelektrophorese von Komplexen der seltenen Erden mit Hydroxyaminos�uren. Mikrochim Acta 1966, 54, 63. <https://doi.org/10.1007/BF01217434>
• Jokl Vladimir: Studium der komplexverbindungen in lösung mittels papierelektrophorese. Journal of Chromatography A 1964, 13, 451. <https://doi.org/10.1016/S0021-9673(01)95141-6>
• El-Marsafy M. K., Řeháček Z., Zenab Abdel-Gawad: Electrochromatography of amino acid mixtures in fermentation liquors. Folia Microbiol 1963, 8, 362. <https://doi.org/10.1007/BF02906034>
• Ivanov Ch., Alexiev B., Krsteva M.: On the interaction of insulin with raney nickel. Biochimica et Biophysica Acta 1963, 69, 195. <https://doi.org/10.1016/0006-3002(63)91250-2>
• Adloff J.-P., Bertrand R.: Separation de radioéléments par électrophorèse sur papier à haute tension. Journal of Electroanalytical Chemistry (1959) 1963, 5, 461. <https://doi.org/10.1016/0022-0728(63)80054-6>
• Mistretta A.G.: Progress in fractionation procedures. I. Differential migration methods: 1960. Microchemical Journal 1961, 5, 305. <https://doi.org/10.1016/0026-265X(61)90004-2>