ABSTRACT
A 12 years old child had an increase of intra cranial pressure secondary to a large pinealoblastoma. A ventriculo peritoneal shunt procedure was performed followed several days later by a partial resection of the pinealoblastoma. One year later, ultrasound and computed tomography examinations discovered a solid mass in the pelvis. At surgery it appeared to be a metastasis of the pinealoblastoma. It is a very seldom complication of the shunt and various mechanisms are discussed.
Subject(s)
Brain Neoplasms/surgery , Cerebrospinal Fluid Shunts/adverse effects , Peritoneal Neoplasms/secondary , Pinealoma/secondary , Antineoplastic Combined Chemotherapy Protocols/therapeutic use , Brain Neoplasms/pathology , Child , Female , Humans , Peritoneal Neoplasms/pathology , Peritoneal Neoplasms/surgery , Peritoneum/surgery , Pinealoma/pathology , Pinealoma/surgery , Tomography, X-Ray , UltrasonographySubject(s)
Epitopes , Erythrocruorins/immunology , Hemoglobins/immunology , Hypersensitivity/immunology , Peptides/immunology , Amino Acid Sequence , Animals , Binding, Competitive , Bronchial Provocation Tests , Chironomidae , Humans , Hypersensitivity/diagnosis , Hypersensitivity, Immediate/diagnosis , Radioallergosorbent Test , Skin TestsABSTRACT
The sequence analysis of the monomeric hemoglobin CTT IV is given. The primary structure was determined by automatic Edman degradation of the protein and of peptides obtained by enzymatical or by chemical cleavages. The protein chain consists of 136 amino acids. The primary structure is compared with the primary structure of the human beta-chains and of the monomeric hemoglobin CTT III.
Subject(s)
Chironomidae/analysis , Diptera/analysis , Erythrocruorins , Hemoglobins , Amino Acid Sequence , Cyanogen Bromide , Humans , Peptide Fragments/analysis , Species Specificity , TrypsinABSTRACT
The primary structure of the monomeric hemoglobin (Erythrocruorin) CTT IV from larvae of Chironomus thummi thummi (Diptera) is presented. The sequence was determined automatically. The primary structure is compared with human alpha-globin-chain.
Subject(s)
Chironomidae/analysis , Diptera/analysis , Erythrocruorins , Hemoglobins , Amino Acid Sequence , Animals , Cyanogen Bromide , Humans , Larva/analysis , Peptide Fragments/analysis , Species Specificity , TrypsinABSTRACT
Cyanogen bromide peptides are modified with arginine (free base) at the C-terminal homoserin lactone. This modification makes the peptides more hydrophilic. In that way the degradation is possible up to homoserine and the C-terminal arginine. The phenylthiohydantoin derivatives of homoserine and arginine can be detected in good yields by thin-layer or high performance liquid chromatography. The automatic Edman degradation is investigated under various conditions.
Subject(s)
Arginine/metabolism , Cyanogen Bromide/metabolism , Peptide Chain Termination, Translational , Amino Acid Sequence , Chromatography, Liquid , Chromatography, Thin Layer , Phenylthiohydantoin/metabolismABSTRACT
This paper describes the covalent fixation and hydrophilisation of homoserin lactone peptides enabling complete C-terminal sequencing in the squenator. Dimethylformamide, dimethylsulfoxide and 6M guanidine hydrochloride in water were used as solvents, ethylendiamine, hexamethylendiamine and histamine base as amino components. The diamine peptide derivative was reacted with the hydrophilic isothiocyanates I and IV, the fixed peptide was sequenced to the C-terminal amino acid, Histamine reacted particularly well and the program with 0.1N quadrol and the hydrophobic buffers was especially suitable for this derivative. The phenylthiohydantoin derivative of homoserine was proven in good yields. The application of this method is suggested.