An improved method of deprotection in solid phase peptide synthesis is disclosed. In particular the deprotecting composition is added in high concentration and small volume to the mixture of the coupling solution, the growing peptide chain, and any excess activated acid from the preceding coupling cycle, and without any draining step between the coupling step of the previous cycle and the addition of the deprotection composition for the successive cycle. Thereafter, the ambient pressure in the vessel is reduced with a vacuum pull to remove the deprotecting composition without any draining step and without otherwise adversely affecting the remaining materials in the vessel or causing problems in subsequent steps in the SPPS cycle.

An improved method of deprotection in solid phase peptide synthesis is disclosed. In particular the deprotecting composition is added in high concentration and small volume to the mixture of the coupling solution, the growing peptide chain, and any excess activated acid from the preceding coupling cycle, and without any draining step between the coupling step of the previous cycle and the addition of the deprotection composition for the successive cycle. Thereafter, the ambient pressure in the vessel is reduced with a vacuum pull to remove the deprotecting composition without any draining step and without otherwise adversely affecting the remaining materials in the vessel or causing problems in subsequent steps in the SPPS cycle.

Provided are a method for extracting a hirudin mutant, HV2-Lys47, from a fermentation broth of the hirudin mutant HV2-Lys47 produced by the fermentation of Escherichia coli, and purifying same, the use of the hirudin mutant HV2-Lys47 in an anticoagulated blood collection tube, and an anticoagulated blood collection tube containing the hirudin mutant HV2-Lys47. In the purification method, a membrane technology and a primary column chromatography technology are used to obtain the hirudin mutant HV2-Lys47.

Provided are a method for extracting a hirudin mutant, HV2-Lys47, from a fermentation broth of the hirudin mutant HV2-Lys47 produced by the fermentation of Escherichia coli, and purifying same, the use of the hirudin mutant HV2-Lys47 in an anticoagulated blood collection tube, and an anticoagulated blood collection tube containing the hirudin mutant HV2-Lys47. In the purification method, a membrane technology and a primary column chromatography technology are used to obtain the hirudin mutant HV2-Lys47.

Provided are a Haemadipsa sylvestris antithrombotic peptide Sylvestin and the use thereof, falling within the technical field of biomedicine. The Haemadipsa sylvestris antithrombotic peptide sylvestin can inhibit FXIIa and kallikrein, has anti-thrombus/infarction effects and alleviates injuries caused by cerebral ischemia, and can also be used in the preparation of inhibitors of FXIIa and kallikrein and drugs for anti-thrombus/infarction and anti-cerebral ischemic injuries.

Provided are a Haemadipsa sylvestris antithrombotic peptide Sylvestin and the use thereof, falling within the technical field of biomedicine. The Haemadipsa sylvestris antithrombotic peptide sylvestin can inhibit FXIIa and kallikrein, has anti-thrombus/infarction effects and alleviates injuries caused by cerebral ischemia, and can also be used in the preparation of inhibitors of FXIIa and kallikrein and drugs for anti-thrombus/infarction and anti-cerebral ischemic injuries.

An improved method of deprotection in solid phase peptide synthesis is disclosed. In particular the deprotecting composition is added in high concentration and small volume to the mixture of the coupling solution, the growing peptide chain, and any excess activated acid from the preceding coupling cycle, and without any draining step between the coupling step of the previous cycle and the addition of the deprotection composition for the successive cycle. Thereafter, the ambient pressure in the vessel is reduced with a vacuum pull to remove the deprotecting composition without any draining step and without otherwise adversely affecting the remaining materials in the vessel or causing problems in subsequent steps in the SPPS cycle.

An improved method of deprotection in solid phase peptide synthesis is disclosed. In particular the deprotecting composition is added in high concentration and small volume to the mixture of the coupling solution, the growing peptide chain, and any excess activated acid from the preceding coupling cycle, and without any draining step between the coupling step of the previous cycle and the addition of the deprotection composition for the successive cycle. Thereafter, the ambient pressure in the vessel is reduced with a vacuum pull to remove the deprotecting composition without any draining step and without otherwise adversely affecting the remaining materials in the vessel or causing problems in subsequent steps in the SPPS cycle.

The present application discloses peptides and peptaibols of high purity may be obtained by solid phase peptide synthesis using as the starting resin hydroxy amino acids, hydroxy amino acid amides, hydroxy amino alcohols or small peptides containing hydroxy amino acids attached to polymers through their side chain.

The present application discloses peptides and peptaibols of high purity may be obtained by solid phase peptide synthesis using as the starting resin hydroxy amino acids, hydroxy amino acid amides, hydroxy amino alcohols or small peptides containing hydroxy amino acids attached to polymers through their side chain.