[Investigation of 603 medical staff occupational exposure with blood-borne pathogens].

Objective: To investigate the occupational exposure with blood-borne pathogens of medical staff, and explore the protective strategy. Methods: Using cluster sampling method, 603 medical staff with occupational exposure with blood-borne pathogens were analyzed, from July 2014 to July 2018 in a tertiary hospital. Results: In total of 603 occupational exposure incidents, 70.98% (428/603) were freshmen younger than 30 years old. 48.92% (295/603) nurses. The most cases of occupational exposure were in surgery (35.16%, 212/603) . Sharp injury was the major contact manner (86.90%, 524/603) . Hands were the main contact parts (90.38%, 545/603) . Ward (53.57%, 323/603) and the operating room (22.72%, 137/603) were the high-risk place. The most dangerous actions were needle injection (34.83%, 210/603) , surgery (20.89%, 126/603) and finishing/cleaning items (19.73%, 119/603) . The main items lead to injuries were scalp needles (34.73%, 182/524) . The most exposure source was hepatitis B virus (HBV) which occupied 39.30% (237/603) . Exposure source mainly comes from medical devices containing blood (81.92%, 494/603) . To compared the groups (χ(2)=19.940, P<0.01) and titer (t=-8.592, P<0.01) of hepatitis B surface antibody (HBsAb) before and after used prophylactics, the differences were statistically significant. Conclusion: Comprehensive strategies of occupational exposure protection education, operation norms and monitoring management were effective methods to reduce the occupational exposure in the medical staff with blood-borne pathogens.

[Reconstruction of the shoulder joint function in the older obstetrical palsy].

OBJECTIVE: To study the reconstructional method and effect of shoulder joint function in the older obstetrical palsy with medial rotation contracture deformity. METHODS: From April 1996 to July 1999, 7 patients of older obstetrical palsy were adopted in this study. Among them, there were 5 males and 2 females, aged from 13 to 21 years old. No previous operation history and the main deformity was medial rotation contracture of shoulder. During operation, these patients were treated with "Z"-shape elongation of the tendon of subscapular muscle, transfer of the tendons of latissimus dorsi and teres major muscle to the tendons of supraspinous and infraspinous muscles. RESULTS: Followed up for 6 to 44 months(averaged 19 months), the Gilbert grading and Mallet scoring were 1.57, 7.57 preoperatively versus 3.45, 10.86 postoperatively, the abduction and external rotation of the shoulder joints recovered obviously. CONCLUSION: It is an effective operation for the older obstetrical palsy with medial rotation contracture of shoulder.

Protein-induced changes in nonplanarity of the porphyrin in nickel cytochrome c probed by resonance Raman spectroscopy.

The influence of the protein on the nonplanarity of the macrocycle for nickel(II)-reconstituted cytochrome c (NiCyt-c) has been investigated with pH-dependent resonance Raman and UV-visible absorption spectroscopy and molecular mechanics calculations. The spectra reveal that NiCyt-c near neutral pH has axially coordinated Ni, but below pH 3 and above pH 12, four-coordinate species predominate. The shape of the structure-sensitive Raman line nu10 of NiCyt-c is asymmetric and broad and it changes with pH. This broad line can be decomposed well into at least two sublines, a low-frequency line that results from a nonplanar conformer and a high-frequency line that arises from a nearly planar conformer. Upon lowering the pH from 3.0 to 1.0, the amount of the nonplanar conformer decreases relative to that of the planar conformer. The decreased nonplanarity can be accounted for in terms of the disruption of a hydrogen-bonding network in the peptide backbone upon lowering the pH. Molecular mechanics (MM) calculations on iron(III) and nickel(II) microperoxidase 5 (MP-5) as well as some model heme derivatives have been carried out in order to locate the part of the protein that causes the heme distortion observed in the X-ray crystal structures of cytochromes c. The energy-optimized structures of MP-5 and the model compounds were analyzed using the normal-coordinate structural decomposition method to specify and quantify the out-of-plane macrocyclic distortions. MM calculations for MP-5 show that two hydrogen bonds formed between the amide groups in the peptide backbone are important in maintaining the ruffled deformation of the macrocycle. All evidence presented supports the hypothesis that the nonplanar distortion of the porphyrin of cytochromes c is largely maintained by a relatively small protein segment including the cysteines, the amino acids between the cysteines, and the adjacent histidine ligand. Hydrogen bonding within the backbone of this segment is important in maintaining the conformation of the peptide that induces the porphyrin distortion.