Automatische Säulen-Chromatographie von Peptiden im Nanomolmaßstab

Machleidt, Werner; Kerner, W.; Otto, Joachim

doi:10.1007/bf00546373

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1970

1977

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Cited by 8 publications

(2 citation statements)

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“…Because from a total of 5.5 ,umol of Bdellin B-3 all sequence studies had to be done, nanomole minus (13)(14)(15)(16)(17)(18)(19)(20)(21) b Cleavage by trypsin (try) or trypsin and chymotrypsin (try/thy) c In stored fractions; in freshly prepared fractions 6 histidine residues were found methods were applied for peptide chromatography [25] , amino acid analysis [26] and sequence studies [27].…”

Section: Experimental and Resultsmentioning

confidence: 99%

Structural homology of a trypsin‐plasmin inhibitor from leeches (bdellin B‐3) with secretory trypsin inhibitors from mammals

Krejci¹,

Fritz²

1976

FEBS Letters

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Section: Experimental and Resultsmentioning

confidence: 99%

Structural homology of a trypsin‐plasmin inhibitor from leeches (bdellin B‐3) with secretory trypsin inhibitors from mammals

Krejci¹,

Fritz²

1976

FEBS Letters

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“…An insoluble residue of undigested protein or insoluble peptides was centrifuged off. The peptides were analyzed by automatic chromatography on a 0.1 × 50 cm column with the cation exchange Aminex A 6 (Bio-Rad Laboratories, Richmond, California), according to a method developed in our laboratory [12]. The peptides in the effluent are detected by continuous reaction with trinitrobenzene sulfonic acid and flow-cell photometry at 334 nm.…”

Section: Methodsmentioning

confidence: 99%