ABSTRACT
Adolescents are frequently victims of sexual assault, often by a previously known assailant. This article discusses the initial management of adolescents who have been sexually assaulted, including obtaining the history and performing a careful physical examination, forensic evidence collection, and medical and psychologic therapy.
Subject(s)
Rape , Adolescent , Contraceptives, Postcoital/therapeutic use , Female , Humans , Medical History Taking , Physical Examination , Rape/diagnosis , Rape/psychology , Sexually Transmitted Diseases/diagnosis , Sexually Transmitted Diseases/etiology , Surveys and QuestionnairesSubject(s)
Heart Arrest/therapy , Medical Futility , Resuscitation , Thoracic Injuries/therapy , Wounds, Nonpenetrating/therapy , Wounds, Stab/therapy , Child , Emergency Medicine , Heart Arrest/etiology , Humans , Male , Severity of Illness Index , Thoracic Injuries/complications , Wounds, Nonpenetrating/classification , Wounds, Stab/complicationsABSTRACT
STUDY OBJECTIVE: To determine the accuracy of the esophageal detector device (EDD) in predicting correct endotracheal tube (ETT) placement in a newborn-piglet model. METHODS: We used an EDD, comprising a 5-, 10- or 20-mL syringe attached to 4-mm tubing fitted to a 15-mm ETT adapter, to aspirate gas from cuffed or uncuffed ETTs placed in the trachea or esophagus of each newborn piglet. During aspiration, we noted any resistance encountered while pulling back the plunger of the syringe and recorded the total volume of gas aspirated into the syringe. A positive test, signifying tracheal ETT placement, was defined as the ability to freely aspirate gas without resistance and the aspiration of enough gas to fill the entire volume of the syringe. A negative test, signifying esophageal ETT placement, was defined as resistance encountered during the aspiration of gas into the syringe and rebound of the syringe plunger, leading to aspiration of a volume of gas less than the total volume of the syringe. RESULTS: We conducted 444 trials (222 for uncuffed ETTs, 222 for cuffed ETTs). ETT size ranged from 3.0 to 4.5 mm. For cuffed ETTs, the 5-mL syringe had a sensitivity of 100% and a specificity of 5%, the 10-mL syringe had a sensitivity of 95% and a specificity of 16%, and the 20-mL syringe had a sensitivity of 86% and a specificity of 97%. For uncuffed ETTs, the 5-mL syringe had a sensitivity of 100% and a specificity of 5%, the 10-mL syringe had a sensitivity of 97% and a specificity of 24%, and the 20-mL syringe had a sensitivity of 81% and a specificity of 100%. CONCLUSION: No syringe had 100% sensitivity and specificity in correctly predicting ETT placement. The 20-mL syringe had the highest combination of sensitivity and specificity. Further studies are warranted to determine whether the EDD using a 20-mL syringe would aid in the prediction of correct ETT placement in the pediatric population.
Subject(s)
Intubation, Intratracheal , Syringes , Animals , Animals, Newborn , Predictive Value of Tests , Pressure , Sensitivity and Specificity , SwineSubject(s)
Conscious Sedation , Emergency Treatment , Pediatrics , Spinal Puncture , Tomography, X-Ray Computed , Child , Child, Preschool , Female , Humans , Infant , Male , Patient Selection , Wounds, Penetrating/surgeryABSTRACT
Owing to its lower incidence in young children, appendicitis is not as often thought of as a common cause of abdominal pain and vomiting in this age group. However, because of its higher incidence of morbidity (perforation and peritonitis), it should be considered in any young child with either significant abdominal pain or vomiting, even in the presence of another plausible etiology such as pneumonia.
Subject(s)
Appendicitis/complications , Appendicitis/diagnosis , Pneumonia/etiology , Shock/etiology , Appendicitis/pathology , Appendicitis/surgery , Child, Preschool , Gangrene , Humans , Male , Peritonitis/etiology , Postoperative Complications , Rupture , Shock/prevention & control , Shock/therapyABSTRACT
During 7 years of screening for hemoglobin variants, over 75 rare variants have been characterized. Of these, 18 were described for the first time. This report presents tabulated data regarding the structural and functional defects that were observed, information on the ethnic origin, and other special properties exhibited by these variants. The strategy and procedures for characterizing these variants are also summarized.
Subject(s)
Hemoglobins, Abnormal/analysis , Centers for Disease Control and Prevention, U.S. , Globins , Humans , Macromolecular Substances , Mass Screening , United StatesSubject(s)
Alanine/analogs & derivatives , Hemoglobins, Abnormal , Valine , Adult , Amino Acids/analysis , Carbon Monoxide/blood , Female , Heme , Hemoglobin A , Hemoglobins, Abnormal/metabolism , Humans , Hydrogen-Ion Concentration , Kinetics , Magnetic Resonance Spectroscopy , Male , Mass Spectrometry , Oxygen/blood , Pedigree , Peptide Fragments/analysis , Phytic AcidABSTRACT
Hb S Travis is a previously undescribed sickling hemoglobin with two amino acid substitutions in the beta chain: beta6 Glu leads to Val and beta142 Ala leads to Val. The beta6 Glu leads to Val mutation imparts to Hb S Travis the characteristic properties of sickling hemoglobin, namely its association with erythrocyte sickling, the insolubility of the hemoglobin in the reduced form, and a minimum gelling concentration value identical to Hb S. Unlike Hb S, Hb S Travis exhibits an increased oxygen affinity and a decreased affinity for 2,3-bisphosphoglycerate and inositol hexakisphosphate. In addition, the variant hemoglobin's tendency to autoxidize and its mechanical precipitability suggest that there are conformational differences between Hb S and Hb S Travis.
Subject(s)
Hemoglobin, Sickle , Alanine , Amino Acids/analysis , Anemia, Sickle Cell/blood , Anemia, Sickle Cell/genetics , Female , Genetic Variation , Glutamates , Humans , Hydrogen-Ion Concentration , Kinetics , Male , Oxygen/blood , Pedigree , Peptide Fragments/analysis , ValineSubject(s)
Hemoglobins, Abnormal , Amino Acids/analysis , Binding Sites , Child , Hemoglobin A , Heterozygote , Humans , Hydrogen-Ion Concentration , Macromolecular Substances , Male , Oxygen/blood , Protein BindingABSTRACT
Procedures are described for the preparation of cyanogen bromide and maleyl peptides of the alpha and beta chains of human hemoglobin. These relatively large peptides have facilitated application of automated sequencing techniques to determine mutations in the primary structure of abnormal hemoglobins.
Subject(s)
Hemoglobin A , Hemoglobins , Amino Acid Sequence , Cyanogen Bromide , Humans , Maleic Anhydrides , Methods , Peptide Fragments/isolation & purificationABSTRACT
Hemoglobin Lufkin was found in a Black-American family. Structural analysis of the abnormal hemoglobin indicates a substitution of aspartic acid for glycine at position 29 in the beta chain. Marked instability of the variant hemoglobin is demonstrated by the rapid formation of inclusion bodies upon exposure of the red cells to redox dyes and by the large percentage of precipitated hemoglobin at 65 degrees C. The oxygen affinity, the Bohr effect, and the degree of cooperativity of Hb Lufkin and Hb A are similar over the physiologic pH range. However, at acid pH the oxygen affinity of the variant is increased. Unlike several other reported variants in the B helix, Hb Lufkin is not associated with methemoglobinemia.
Subject(s)
Amino Acids , Aspartic Acid/metabolism , Genetic Variation , Glycine/metabolism , Hemoglobins, Abnormal/isolation & purification , Anemia, Hemolytic/blood , Child , Electrophoresis, Cellulose Acetate , Globins/isolation & purification , Humans , Hydrogen-Ion Concentration , Male , Oxygen/metabolism , Peptides/isolation & purification , TexasABSTRACT
Hemoglobin Fannin-Lubbock was found in a 9-year-old Mexican-American female. The abnormal hemoglobin was detected as a fast-moving variant by electrophoresis on cellulose acetate at pH 8.4. Structural analysis indicated a substitution in the beta-chain of aspartic acid for glycine at position 119, a position involved in the alpha1beta1 contact of the hemoglobin tetramer. This contact between unlike chains is larger and undergoes a smaller shift during the process of oxygenation and deoxygenation that the alpha1beta2 contact (Perutz, M.F., Muirhead, H., Cox, J.M. and Goaman, L.C.G. (1968) Nature 219, 131-139). Mutations in this contact tend to cause slight or no changes in functional behavior. Apart from a mild anemia, the propositus did not exhibit any obvious clinical symptoms.
Subject(s)
Hemoglobins, Abnormal , Amino Acids/analysis , Child , Diphosphoglyceric Acids/blood , Electrophoresis, Cellulose Acetate , Female , Genetic Variation , Hemoglobin A , Humans , Hydrogen-Ion Concentration , Macromolecular Substances , Male , Pedigree , Protein BindingABSTRACT
Hemoglobin Providence Asn and Hemoglobin Providence Asp are two abnormal hemoglobins which apparently arise from a single genetic change that substitutes asparagine for lysine at position 82 (EF6) in the beta chain of human hemoglobin. The second form appears to be thr result of a partial in vivo deamidation of the asparagine situated at position beta 82. Cellulose acetate and citrate agar electrophoresis of hemolysates from patients with this abnormality shows three bands. Globin chain electrophoresis at acid and alkaline pH shows three beta chains. These three chains correspond to the normal beta A chain and two abnormal beta chains. Sequence analysis indicates that the two abnormal chains differ from beta A at only position beta 82. In the two abnormal chains, the residue which is normally lysine is substituted either by asparagine or by aspartic acid. These substitutions are notable because beta 82 lysine is one of the residues involved in 2,3-diphosphoglycerate binding. Additionally, beta 82 lysine is typically invariant in hemoglobin beta chain sequences. Sequence data on the two forms of Hemoglobin Providence are given in this paper. The functional properties of these two forms are described in the next paper.
Subject(s)
Hemoglobins, Abnormal , Adult , Amino Acids/analysis , Asparagine , Aspartic Acid , Blood Protein Electrophoresis , Female , Genetic Variation , Hemoglobins, Abnormal/isolation & purification , Humans , Male , Pedigree , Peptide Fragments/analysisABSTRACT
Cellulose acetate electrophoresis at pH 8.4 showed a hemoglobin variant with the mobility of hemoglobin S in a Canadian family. Sequence analysis revealed that histidine was substituted for aspartic acid at position 64 in the alpha-chain. This variant was found in association with a beta-thalassemia trait condition.
Subject(s)
Hemoglobins, Abnormal/analysis , Thalassemia/blood , Amino Acids/analysis , Child, Preschool , Humans , India , Male , Thalassemia/geneticsABSTRACT
A new hemoglobin mutant was detected as a fast-moving variant on cellulose acetate electrophoresis at pH 8.4. The mutation is in the alpha-chain at position 127, where lysine is substituted by asparagine. This is an external residue, and mutation at this site does not lead to any altered physiologic function of the hemoglobin.
Subject(s)
Hemoglobins, Abnormal/analysis , Adult , Amino Acids/analysis , Female , HumansABSTRACT
The first reported case of hemoglobin S and C Harlem in an individual is described. The patient, a 35-yr-old female, had numerous crises during adolescence and early adulthood, but these occurred more infrequently as she grew older. Chemical evidence is presented for the characterization of both variant hemoglobins. The clinical course of this individual with Hb S in combination with Hb C Harlem appears to be similar to that for persons with sickle cell anemia.